Drupal-Biblio13Drupal-Biblio5<style face="normal" font="default" size="100%">2.06 - Iron-sulfur clusters – functions of an ancient metal site</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Biochemical characterization of AniA from Neisseria gonorrhoeae</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Photomodulation of ultrastable host–guest complexes in water and their application in light-controlled steroid release</style>Drupal-Biblio17<style face="normal" font="default" size="100%">OrpR is a σ54-dependent activator using an iron-sulfur cluster for redox sensing in Desulfovibrio vulgaris Hildenborough</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Acrylamide-hemoglobin adduct: A spectroscopic study</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The effect of pH on Marinobacter hydrocarbonoclasticus denitrification pathway and nitrous oxide reductase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study</style>Drupal-Biblio5<style face="normal" font="default" size="100%">Transition Metals and Sulfur – A Strong Relationship for Life5. The Tetranuclear Copper-Sulfide Center of Nitrous Oxide Reductase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The bacterial Mrp<inf>ORP</inf> is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis</style>Drupal-Biblio6<style face="normal" font="default" size="100%">Reduction of hydrogen peroxide in gram-negative bacteria – bacterial peroxidases</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Source and reduction of nitrous oxide</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Genomic organization, gene expression and activity profile of Marinobacter hydrocarbonoclasticus denitrification enzymes</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin</style>Drupal-Biblio17<style face="normal" font="default" size="100%">YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity</style>Drupal-Biblio17<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>Drupal-Biblio17<style face="normal" font="default" size="100%">Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The catalytic cycle of nitrous oxide reductase — The enzyme that catalyzes the last step of denitrification</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Insights into the recognition and electron transfer steps in nitric oxide reductase from Marinobacter hydrocarbonoclasticus</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Spectroscopic Definition of the CuZ0 Intermediate in Turnover of Nitrous Oxide Reductase and Molecular Insight into the Catalytic Mechanism</style>Drupal-Biblio13<style face="normal" font="default" size="100%">CHAPTER 11: Electron Transfer and Molecular Recognition in Denitrification and Nitrate Dissimilatory Pathways</style>Drupal-Biblio13<style face="normal" font="default" size="100%">CHAPTER 1: A Bird's Eye View of Denitrification in Relation to the Nitrogen Cycle</style>Drupal-Biblio13<style face="normal" font="default" size="100%">CHAPTER 7: Insights into Nitrous Oxide Reductase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The small iron-sulfur protein from the ORP operon binds a [2Fe-2S] cluster</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Orange protein from Desulfovibrio alaskensis G20: insights into the Mo-Cu cluster protein-assisted synthesis</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Predicting Protein-Protein Interactions Using BiGGER: Case Studies</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Resonance assignment of DVU2108 that is part of the Orange Protein complex in Desulfovibrio vulgaris Hildenborough</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Protonation state of the Cu4S2 CuZ site in nitrous oxide reductase: redox dependence and insight into reactivity</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Incorporation of molybdenum in rubredoxin: models for mononuclear molybdenum enzymes</style>Drupal-Biblio47<style face="normal" font="default" size="100%">HCN Channels: The Molecular Basis for their cAMP-TRIP8b Regulation</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function</style>Drupal-Biblio47<style face="normal" font="default" size="100%">INSIGHTS INTO THE CATALYTICCYCLE OF Pseudomonas nautica NITROUS OXIDE REDUCTASE</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Mo-Cu metal cluster formation and binding in an orange protein isolated from Desulfovibrio gigas</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Synthesis and characterization of [S2MoS2Cu(n-SPhF)](2-) (n = o, m, P) clusters: Potential F-19-NMR structural probes for Orange Protein</style>Drupal-Biblio47<style face="normal" font="default" size="100%">The Auxiliary Subunit TRIP8B Inhibits the Binding of CAMP to HCN2 Channels Through an Allosteric Mechanism</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Determination of the active form of the tetranuclear copper sulfur cluster in nitrous oxide reductase</style>Drupal-Biblio17<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>Drupal-Biblio47<style face="normal" font="default" size="100%">Electronic structure and reactivities of resting and intermediate forms of the tetranuclear copper cluster in nitrous oxide reductase</style>Drupal-Biblio47<style face="normal" font="default" size="100%">Metal substituted rubredoxins: a sulfur rich coordination site as models for metalloenzymes</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Superoxide reductase: different interaction modes with its two redox partners</style>Drupal-Biblio17<style face="normal" font="default" size="100%">(1)H, (13)C and (15)N resonance assignment of the soluble form of the Lipid-modified Azurin from Neisseria gonorrhoeae</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Copper-substituted forms of the wild type and C42A variant of rubredoxin</style>Drupal-Biblio47<style face="normal" font="default" size="100%">Physiological and Biochemical insights into the E. coli cytochrome c peroxidase</style>Drupal-Biblio47<style face="normal" font="default" size="100%">Structural rearrangements occurring on HCN2 CNBD domain upon cAMP binding</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Nitrous oxide reductase</style>Drupal-Biblio5<style face="normal" font="default" size="100%">Iron-sulfur centers: new roles for ancient metal sites</style>
Drupal-Biblio47<style face="normal" font="default" size="100%">Marinobacter hydrocarbonoclasticus is an aerobic denitrifier</style>Drupal-Biblio5<style face="normal" font="default" size="100%">Nitrous oxide reductase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Rearrangement of Mo-Cu-S Cluster Reflects the Structural ­Instability of Orange Protein Cofactor</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Synthesis of MoS4 (2-)-M (M=Cu and Cd) Clusters: Potential NMR Spectroscopic Structural Probes for the Orange Protein</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Analysis of resonance Raman data on the blue copper site in pseudoazurin: Excited state pi and sigma charge transfer distortions and their relation to ground state reorganization energy</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Biochemical characterization of the purple form of Marinobacter hydrocarbonoclasticus nitrous oxide reductase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Gd(III) chelates as NMR probes of protein-protein interactions. Case study: rubredoxin and cytochrome c3</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The Anaerobe-Specific Orange Protein Complex of Desulfovibrio vulgaris Hildenborough Is Encoded by Two Divergent Operons Coregulated by sigma(54) and a Cognate Transcriptional Regulator</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Artefacts induced on c-type haem proteins by electrode surfaces</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The tetranuclear copper active site of nitrous oxide reductase: the CuZ center</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The electron transfer complex between nitrous oxide reductase and its electron donors</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The 1.4 angstrom resolution structure of Paracoccus pantotrophus pseudoazurin</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Pressure Perturbation Calorimetry and the Thermodynamics of Noncovalent Interactions in Water: Comparison of Protein-Protein, Protein-Ligand, and Cyclodextrin-Adamantane Complexes</style>Drupal-Biblio17<style face="normal" font="default" size="100%">A new CuZ active form in the catalytic reduction of N2O by nitrous oxide reductase from Pseudomonas nautica</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Rubredoxin as a paramagnetic relaxation-inducing probe</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Isolation and characterization of a new Cu-Fe protein from Desulfovibrio aminophilus DSM12254</style>Drupal-Biblio17<style face="normal" font="default" size="100%">A variable temperature spectroscopic study on Paracoccuspantotrophus pseudoazurin: protein constraints on the blue Cu site</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from Desulfovibrio gigas</style>Drupal-Biblio17<style face="normal" font="default" size="100%">The electron transfer complex between D. gigas Superoxide Reductase and Rubredoxin</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Molecular interactions/electron transfer protein complexes using Docking algorithms, spectroscopy (NMR) and site direct mutagenesis</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from Desulfovibrio gigas. (vol F65, pg 730, 2009)</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Electron transfer complex between nitrous oxide reductase and cytochrome c(552) from Pseudomonas nautica: Kinetic, nuclear magnetic resonance, and docking studies</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Enzymatic activity mastered by altering metal coordination spheres</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Calcium-dependent heme structure in the reduced forms of the bacterial cytochrome c peroxidase from Paracoccus pantotrophus</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by P-pantotrophus pseudoazurin: kinetics of intermolecular electron transfer</style>Drupal-Biblio17<style face="normal" font="default" size="100%">NMR assignment of the apo-form of a Desulfovibrio gigas protein containing a novel Mo-Cu cluster</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Structure and mechanism in the bacterial dihaem cytochrome c peroxidases</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Paracoccus pantotrophus pseudoazurin is an electron donor to cytochrome c peroxidase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans containing more than one cytochrome</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Structural changes in the calcium-dependent activation of the di-heme cytochrome c peroxidase of Paracoccus pantotrophus</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Calcium-dependent conformation of a heme and fingerprint peptide of the diheme cytochrome c peroxidase from Paracoccus pantotrophus</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Cytochrome c peroxidase and its redox partners - binary and ternary complexes</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Cytochrome c peroxidase as a model system to study electron transfer complexes</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Structural changes associated with calcium-dependent activation of the di-heme cytochrome c peroxidase of Paracoccus pantotrophus</style>