<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">F Gomes</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">J.A. Loureiro</style></author><author><style face="normal" font="default" size="100%">M.C. Pereira</style></author><author><style face="normal" font="default" size="100%">C Delerue-Matos</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">S Morais</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Biosensor for direct bioelectrocatalysis detection of nitric oxide using nitric oxide reductase incorporated in carboxylated single-walled carbon nanotubes/lipidic 3 bilayer nanocomposite</style></title><secondary-title><style face="normal" font="default" size="100%">Bioelectrochem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1016/j.bioelechem.2019.01.010</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">127</style></volume><pages><style face="normal" font="default" size="100%">76-86</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/bioelectrochem-2019-127-76.pdf&quot;&gt;https://docentes.fct.unl.pt/lblm/files/bioelectrochem-2019-127-76.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Cordas, C</style></author><author><style face="normal" font="default" size="100%">M. Campaniço</style></author><author><style face="normal" font="default" size="100%">R. Baptista</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Direct electrochemical reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase</style></title><secondary-title><style face="normal" font="default" size="100%">J Inorg Biochem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1016/j.jinorgbio.2019.110694</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">196</style></volume><pages><style face="normal" font="default" size="100%">110694</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/jib-2019-196-110694.pdf&quot;&gt;https://docentes.fct.unl.pt/lblm/files/jib-2019-196-110694.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">F Gomes</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">Cordas, C</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">C Delerue-Matos</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">S Morais</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Electroanalytical characterization of the direct Marinobacter hydrocarbonoclasticus nitric oxide reductase-catalysed nitric oxide and dioxygen reduction</style></title><secondary-title><style face="normal" font="default" size="100%">Bioelectrochem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://dx.doi.org/10.1016/j.bioelechem.2018.08.005</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">125</style></volume><pages><style face="normal" font="default" size="100%">8-14</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/bioelectrochem-2019-125-8.pdf&quot; rel=&quot;nofollow&quot;&gt;https://docentes.fct.unl.pt/lblm/files/bioelectrochem-2019-125-8.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maiti, B. K.</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">NiII-ATCUN-catalyzed tyrosine nitration in the presence of nitrite and sulfite</style></title><secondary-title><style face="normal" font="default" size="100%">Chem Eur J</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1002/chem.201806228</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">25</style></volume><pages><style face="normal" font="default" size="100%">4309-4314</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/chemeurj-2019-25-4309.pdf&quot;&gt;https://docentes.fct.unl.pt/lblm/files/chemeurj-2019-25-4309.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">F Gomes</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">C Delerue-Matos</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">S Morais</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Third-generation electrochemical biosensor based on nitric oxide reductase immobilized in a multiwalled carbon nanotubes/1-n-butyl-3-methylimidazolium tetrafluoroborate nanocomposite for nitric oxide detection</style></title><secondary-title><style face="normal" font="default" size="100%">Sensors Act B Chem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://doi.org/10.1016/j.snb.2019.01.074</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">285</style></volume><pages><style face="normal" font="default" size="100%">445-452</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/sensorsactbchem-2019-285-445.pdf&quot; rel=&quot;nofollow&quot;&gt;https://docentes.fct.unl.pt/lblm/files/sensorsactbchem-2019-285-445.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>5</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, Luisa B.</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mononuclear molybdenum-containing enzymes</style></title><secondary-title><style face="normal" font="default" size="100%">Reference Module in Chemistry, Molecular Sciences and Chemical Engineering</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://dx.doi.org/10.1016/B978-0-12-409547-2.13932-0</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">Elsevier</style></publisher><pages><style face="normal" font="default" size="100%">1-19</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/refmodchem-2018---1.pdf&quot; rel=&quot;nofollow&quot;&gt;https://docentes.fct.unl.pt/lblm/files/refmodchem-2018---1.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">F Gomes</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">Cordas, C</style></author><author><style face="normal" font="default" size="100%">C Delerue-Matos</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">S Morais</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Nitric oxide detection using electrochemical third-generation biosensors – based on heme proteins and porphyrins</style></title><secondary-title><style face="normal" font="default" size="100%">Electroanalysis</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://dx.doi.org/10.1002/elan.201800421</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">30</style></volume><pages><style face="normal" font="default" size="100%">2485-2503</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/electroanalysis-2018-30-2485.pdf&quot; rel=&quot;nofollow&quot;&gt;https://docentes.fct.unl.pt/lblm/files/electroanalysis-2018-30-2485.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">A Samhan-Arias</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">Cordas, C. M.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">C Gutierrez-Merino</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Peroxidase-like activity of cytochrome b5 is triggered upon hemichrome formation in alkaline pH</style></title><secondary-title><style face="normal" font="default" size="100%">BBA - Proteins and Proteomics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://dx.doi.org/10.1016/j.bbapap.2017.09.010</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">1866</style></volume><pages><style face="normal" font="default" size="100%">373-378</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/bba-2018-1866-373.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/bba-2018-1866-373.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: nitrite reduction by molybdoenzymes</style></title><secondary-title><style face="normal" font="default" size="100%">Redox Biol</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.dx.doi.org/10.1016/j.redox.2018.08.020</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">19</style></volume><pages><style face="normal" font="default" size="100%">274-289</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/redoxbiol-2018-19-274.pdf&quot; rel=&quot;nofollow&quot;&gt;https://docentes.fct.unl.pt/lblm/files/redoxbiol-2018-19-274.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maiti, B. K.</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">AJ Moro</style></author><author><style face="normal" font="default" size="100%">Lima, J.C.</style></author><author><style face="normal" font="default" size="100%">Cordas, C. M.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Unusual reduction mechanism of copper in cysteine-rich environment</style></title><secondary-title><style face="normal" font="default" size="100%">Inorg Chem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://dx.doi.org/10.1021/acs.inorgchem.8b00121</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">57</style></volume><pages><style face="normal" font="default" size="100%">8078-8088</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;https://docentes.fct.unl.pt/lblm/files/inorgchem-2018-57-8078.pdf&quot; rel=&quot;nofollow&quot;&gt;https://docentes.fct.unl.pt/lblm/files/inorgchem-2018-57-8078.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>5</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors><secondary-authors><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">A bird’s-eye view of denitrification in relation to the nitrogen cycle</style></title><secondary-title><style face="normal" font="default" size="100%">Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2).</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Xanthine dehydrogenase xanthine oxidase NADH superoxide radical FREE-RADICAL GENERATION LIPID-PEROXIDATION ALDEHYDE OXIDASE OXIDATIVE STRESS KINETIC-PROPERTIES MOLECULAR-OXYGEN ALCOHOL INJURY OXIDOREDUCTASE PURIFICATION</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1039/9781782623762-00001</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">9</style></number><publisher><style face="normal" font="default" size="100%">The Royal Society of Chemistry</style></publisher><volume><style face="normal" font="default" size="100%">39</style></volume><pages><style face="normal" font="default" size="100%">1-10</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;This book is devoted to denitrification, an anaerobic process that is used by a wide range of bacteria for energy generation. The overall process involves nitrate, which is present in soil or water, being reduced to gaseous dinitrogen. This initial chapter aims to place denitrification in the larger context of the nitrogen biogeochemical cycle (a bird’s eye view). Detailed topics are developed through the many following contributions. Denitrification is a landscape for probing the structures, functions and mechanisms of action of a wide range of highly specialised metalloenzymes. These carry out, sequentially, four oxo-transfer reactions: NO&lt;sub&gt;3&lt;/sub&gt;&lt;sup&gt;−&lt;/sup&gt; → NO&lt;sub&gt;2&lt;/sub&gt;&lt;sup&gt;−&lt;/sup&gt; → &lt;sup&gt;˙&lt;/sup&gt;NO → N&lt;sub&gt;2&lt;/sub&gt;O → N&lt;sub&gt;2&lt;/sub&gt;. The environmental implications of these processes are of particular relevance. Nitrate accumulation and the release of nitrous oxide into the atmosphere due to the excessive use of fertilisers in agriculture are examples of two environmental problems in which denitrification plays a central role.&lt;/p&gt;
&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/rsc_book-denitrification-2017-chap_1.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/rsc_book-denitrification-2017-chap_1.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>5</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors><secondary-authors><author><style face="normal" font="default" size="100%">Hanson, G</style></author><author><style face="normal" font="default" size="100%">Berliner, LJ</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">EPR spectroscopy on mononuclear molybdenum-containing enzymes</style></title><secondary-title><style face="normal" font="default" size="100%">Future Directions in Metalloprotein and Metalloenzyme Research, Biological Magnetic Resonance, Vol. 33 (ISBN: 978-3-319-59100-1)</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1007/978-3-319-59100-1_4</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">6</style></number><publisher><style face="normal" font="default" size="100%">Springer Publishers</style></publisher><pub-location><style face="normal" font="default" size="100%">Cham</style></pub-location><volume><style face="normal" font="default" size="100%">12</style></volume><pages><style face="normal" font="default" size="100%">100-130</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The biological relevance of molybdenum was demonstrated in the early 1950s-1960s, by Bray, Beinert, Lowe, Massey, Palmer, Ehrenberg, Pettersson, Vänngård, Hanson and others, with ground-breaking studies performed, precisely, by electron paramagnetic resonance (EPR) spectroscopy. Those earlier studies, aimed to investigate the mammalian xanthine oxidase and avian sulfite oxidase enzymes, demonstrated the surprising biological reduction of molybdenum to the paramagnetic Mo&lt;sup&gt;5+&lt;/sup&gt;. Since then, EPR spectroscopy, alongside with other spectroscopic methods and X-ray crystallography, has contributed to our present detailed knowledge about the active site structures, catalytic mechanisms and structure/activity relationships of the molybdenum-containing enzymes.&lt;br /&gt;This Chapter will provide a perspective on the contribution that EPR spectroscopy has made to some selected systems. After a brief overview on molybdoenzymes, the Chapter will be focused on the EPR studies of mammalian xanthine oxidase, with a brief account on the prokaryotic aldehyde oxidoreductase, nicotinate dehydrogenase and carbon monoxide dehydrogenase, vertebrate sulfite oxidase, and prokaryotic formate dehydrogenases and nitrate reductases.&lt;/p&gt;
&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/epr_book-chap_4.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/epr_book-chap_4.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">R. Viveiros</style></author><author><style face="normal" font="default" size="100%">FM Dias</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">W Heggie</style></author><author><style face="normal" font="default" size="100%">Casimiro, T.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Green strategy to produce large core-shell affinity beads for gravity-driven API purification processes</style></title><secondary-title><style face="normal" font="default" size="100%">J Ind Eng Chem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://dx.doi.org/10.1016/j.jiec.2017.06.012</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">54</style></volume><pages><style face="normal" font="default" size="100%">341-349</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/jiengchem-2017-54-341.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/jiengchem-2017-54-341.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maiti, B. K.</style></author><author><style face="normal" font="default" size="100%">Almeida, R. M.</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">JJG Mura</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Insights into the molybdenum/copper heterometallic cluster assembly in the orange protein: probing intermolecular interactions with an artificial metal-binding ATCUN tag</style></title><secondary-title><style face="normal" font="default" size="100%">Inorg Chem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://dx.doi.org/10.1021/acs.inorgchem.7b00840</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">56</style></volume><pages><style face="normal" font="default" size="100%"> 8900-8911</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/inorgchem-2017-56-8900.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/inorgchem-2017-56-8900.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>5</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors><secondary-authors><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">Lessons from denitrification for the human metabolism of signalling nitric oxide</style></title><secondary-title><style face="normal" font="default" size="100%">Metalloenzymes in Denitrification: Applications and Environmental Impacts, RSC Metallobiology Series No. 9 (ISBN: 978-1-78262-376-2).</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1039/9781782623762-00419</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">The Royal Society of Chemistry</style></publisher><volume><style face="normal" font="default" size="100%">41</style></volume><pages><style face="normal" font="default" size="100%">300-320</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The nitric oxide radical ˙NO (NO) is a signalling molecule involved in several physiological processes in humans, including vasodilation, immune response, neurotransmission, platelet aggregation, apoptosis and gene expression. Undue normal conditions, NO synthases catalyse the formation of NO from l-arginine and dioxygen. Yet, upon a hypoxic event, when the decreased dioxygen concentration compromises NO synthase activity, cells can generate NO from another source: nitrite. Since the late 1990s, it has become clear that nitrite can be reduced back to NO under hypoxic/anoxic conditions. Simultaneously, it was realised that nitrite can exert a significant cytoprotective action in vivo during ischaemia and other pathological conditions. Presently, blood and tissue nitrite are recognised as NO “storage forms” that can be made available in order to maintain NO formation and ensure cell signalling and survival under challenging conditions. To reduce nitrite to NO, human cells can use different metalloproteins that are present in cells for carrying out other functions, including several haemic proteins and molybdoenzymes, forming what we refer to as “non-dedicated nitrite reductases”. In this chapter, two non-dedicated nitrite reductases—xanthine oxidase and myoglobin—will be described, and the human nitrate/nitrite/NO signalling pathway will be discussed within the cellular context and the nitrogen cycle scenario.&lt;/p&gt;
&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/rsc_book-denitrification-2017-chap_17.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/rsc_book-denitrification-2017-chap_17.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>5</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors><secondary-authors><author><style face="normal" font="default" size="100%">Hille, R.</style></author><author><style face="normal" font="default" size="100%">Schulzke, C.</style></author><author><style face="normal" font="default" size="100%">Kirk, M.</style></author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">Molybdenum and tungsten-containing enzymes: an overview</style></title><secondary-title><style face="normal" font="default" size="100%">Molybdenum and Tungsten Enzymes: Biochemistry, RSC Metallobiology Series No. 5 (ISBN: 978-1-78262-089-1). </style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1039/9781782623915-00001</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">The Royal Society of Chemistry</style></publisher><volume><style face="normal" font="default" size="100%">28</style></volume><pages><style face="normal" font="default" size="100%">1-80</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Molybdenum is essential to most organisms, being found in the active site of enzymes that catalyze redox reactions involving carbon, nitrogen and sulfur atoms of key metabolites. Some of the molybdenum-dependent reactions constitute key steps in the global biogeochemical cycles of carbon, nitrogen and sulfur, with particular emphasis on the atmospheric dinitrogen fixation into ammonium. Presently, more than 50 molybdoenzymes are known. The great majority are prokaryotic, with eukaryotes holding only a restricted number of molybdoenzymes. Tungsten, probably because of its limited bioavailability, is less used, being found most often in anaerobic thermophilic prokaryotes.&lt;/p&gt;
&lt;p&gt;This chapter provides an overview on the molybdo- and tungstoenzymes.&lt;br /&gt;
Their physiological context and significance will be described in Section 1.2,where the recent hypothesis that the lack of molybdenum could have been the limiting factor for the life evolution and expansion on early Earth will receive special attention (Section 1.2.1). A brief introduction to the chemical properties that shape the catalytically competent molybdenum/tungsten centres will be made in Section 1.3. In Section 1.4, the enzymes will be grouped in five main families (Sections 1.4.1 to 1.4.5), according to their metal/cofactor structure, and a general view on the structural (section (a)) and mechanistic (section (b)) versatility of each family will be presented. A brief account of novel heteronuclear centres containing molybdenum, whose physiological function is not yet fully understood, will be made in Section 1.4.6. A final outlook on our present knowledge about these enzymes will conclude this chapter.
&lt;/p&gt;
&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/mo_w_enzymes-rsc_book-chap_1.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/mo_w_enzymes-rsc_book-chap_1.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molybdenum and tungsten-containing formate dehydrogenases: aiming to inspire a catalyst for carbon dioxide utilization</style></title><secondary-title><style face="normal" font="default" size="100%">Inorg Chim Acta</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">aldehyde oxidase xanthine oxidase xanthine dehydrogenase purification rat liver FREE-RADICAL GENERATION RABBIT LIVER AFFINITY-CHROMATOGRAPHY O-2-DEPENDENT TYPE DEHYDROGENASE TYPE DEPENDENT TYPE CONVERSION ENZYME MECHANISM CLEAVAGE</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1016/j.ica.2016.07.010</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">1</style></number><volume><style face="normal" font="default" size="100%">455</style></volume><pages><style face="normal" font="default" size="100%">350-363</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/ica-2017-455-350.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/ica-2017-455-350.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maiti, B. K.</style></author><author><style face="normal" font="default" size="100%">Maia, L.</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Protein-Assisted Formation of Molybdenum Heterometallic Clusters: Evidence for the Formation of S2MoS2−M−S2MoS2 Clusters with M = Fe, Co, Ni, Cu, or Cd within the Orange Protein</style></title><secondary-title><style face="normal" font="default" size="100%">Inorg Chem</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2017</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1021/acs.inorgchem.6b02906</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">41</style></number><volume><style face="normal" font="default" size="100%">56</style></volume><pages><style face="normal" font="default" size="100%">2210-2220</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/inorgchem-2017-56-2210.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/inorgchem-2017-56-2210.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Detection of nitric oxide by electron paramagnetic resonance spectroscopy: spin-trapping with iron-dithiocarbamates</style></title><secondary-title><style face="normal" font="default" size="100%">Methods Mol Biol</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1007/978-1-4939-3600-7_8</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">1424</style></volume><pages><style face="normal" font="default" size="100%">81-102</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/methodsmolbiol-2016-1424-81.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/methodsmolbiol-2016-1424-81.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Fonseca, L.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase: a kinetic and mechanistic study</style></title><secondary-title><style face="normal" font="default" size="100%">J Am Chem Soc</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2016</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1021/jacs.6b03941</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">2</style></number><volume><style face="normal" font="default" size="100%">138</style></volume><pages><style face="normal" font="default" size="100%">8834–8846</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/jacs-2016-138-8834.pdf&quot; rel=&quot;nofollow&quot;&gt;http://docentes.fct.unl.pt/lblm/files/jacs-2016-138-8834.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maiti, B. K.</style></author><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Silveira, C. M.</style></author><author><style face="normal" font="default" size="100%">Todorovic, S.</style></author><author><style face="normal" font="default" size="100%">Carreira, C.</style></author><author><style face="normal" font="default" size="100%">Carepo, M. S.</style></author><author><style face="normal" font="default" size="100%">Grazina, R.</style></author><author><style face="normal" font="default" size="100%">Moura, I</style></author><author><style face="normal" font="default" size="100%">Pauleta, S. R.</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Incorporation of molybdenum in rubredoxin: models for mononuclear molybdenum enzymes</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Inorganic Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1007/s00775-015-1268-0</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">821-829</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-821.pdf&quot;&gt;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-821.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Moura, JJG</style></author><author><style face="normal" font="default" size="100%">Bernhardt, PV</style></author><author><style face="normal" font="default" size="100%">Maia, L. B.</style></author><author><style face="normal" font="default" size="100%">Gonzalez, P. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molybdenum and tungsten enzymes: from Biology to chemistry and back</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Inorganic Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1007/s00775-015-1243-9</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">181-182</style></pages><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-181.pdf&quot;&gt;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-181.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, Luisa B.</style></author><author><style face="normal" font="default" size="100%">Moura, Jose J. G.</style></author><author><style face="normal" font="default" size="100%">Moura, Isabel</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molybdenum and tungsten-dependent formate dehydrogenases</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Inorganic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Molybdenum Tungsten Formate oxidation Carbon dioxide reduction Formate-dependent energy metabolism Sulfur-shift</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1007/s00775-014-1218-2</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">287-309</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-287.pdf&quot;&gt;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-287.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, Luisa B.</style></author><author><style face="normal" font="default" size="100%">Pereira, V</style></author><author><style face="normal" font="default" size="100%">Mira, Lurdes</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Nitrite reductase activity of rat and human xanthine oxidase, xanthine dehydrogenase and aldehyde oxidase: evaluation of their contribution to the NO formation in vivo</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1021/bi500987w</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">54</style></volume><pages><style face="normal" font="default" size="100%">685-710</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/biochemistry-2015-54-685.pdf&quot;&gt;http://docentes.fct.unl.pt/lblm/files/biochemistry-2015-54-685.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, Luisa B.</style></author><author><style face="normal" font="default" size="100%">Moura, JJG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Inorganic Chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Molybdenum Nitrite reduction Nitric oxide Cell signalling Moonlighting</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1007/s00775-014-1234-2</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">403-433</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-403_1.pdf&quot;&gt;http://docentes.fct.unl.pt/lblm/files/jbic-2015-20-403_1.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maia, Luisa B.</style></author><author><style face="normal" font="default" size="100%">Moura, Jose J. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">How Biology handles nitrite</style></title><secondary-title><style face="normal" font="default" size="100%">Chemical Reviews</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2014</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1021/cr400518y</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">10</style></number><volume><style face="normal" font="default" size="100%">114</style></volume><pages><style face="normal" font="default" size="100%">5273-5357</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/chemrev-2014-114-5273_0.pdf&quot;&gt;http://docentes.fct.unl.pt/lblm/files/chemrev-2014-114-5273_0.pdf&lt;/a&gt;&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Journal Article</style></work-type></record><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Maiti, Biplab K.</style></author><author><style face="normal" font="default" size="100%">Maia, Luisa B.</style></author><author><style face="normal" font="default" size="100%">Pal, Kuntal</style></author><author><style face="normal" font="default" size="100%">Pakhira, Bholanath</style></author><author><style face="normal" font="default" size="100%">Aviles, Teresa</style></author><author><style face="normal" font="default" size="100%">Moura, Isabel</style></author><author><style face="normal" font="default" size="100%">Pauleta, Sofia R</style></author><author><style face="normal" font="default" size="100%">Nunez, Jose L.</style></author><author><style face="normal" font="default" size="100%">Rizzi, Alberto C.</style></author><author><style face="normal" font="default" size="100%">Brondino, Carlos D.</style></author><author><style face="normal" font="default" size="100%">Sarkar, Sabyasachi</style></author><author><style face="normal" font="default" size="100%">Moura, Jose J. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">One electron reduced square planar bis(benzene-1,2-dithiolato) copper dianionic complex and redox switch by O2/HO-</style></title><secondary-title><style face="normal" font="default" size="100%">Inorganic Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2014</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1021/ic501742j</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">24</style></number><volume><style face="normal" font="default" size="100%">53</style></volume><pages><style face="normal" font="default" size="100%">12799-12808</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;a href=&quot;http://docentes.fct.unl.pt/lblm/files/inorgchem-2014-53-12799.pdf&quot;&gt;http://docentes.fct.unl.pt/lblm/files/inorgchem-2014-53-12799.pdf&lt;/a&gt;&lt;/p&gt;
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