@article {Pamplona:1999ta,
	title = {{Cloning and overexpression of E.Coli fuscoredoxin}},
	journal = {Journal Of Inorganic Biochemistry},
	volume = {74},
	number = {1-4},
	year = {1999},
	pages = {260{\textendash}260},
	author = {Pamplona, A and Pereira, AS and Tavares, P. and Moura, I and Rusnak, F and Moura, JJG}
}
@article {Pauleta:2007ds,
	title = {{NMR assignment of the apo-form of a Desulfovibrio gigas protein containing a novel Mo-Cu cluster}},
	journal = {Biomolecular Nmr Assignments},
	volume = {1},
	number = {1},
	year = {2007},
	pages = {81{\textendash}83},
	abstract = {We report the 98\% assignment of the apo-form of an orange protein, containing a novel Mo-Cu cluster isolated from Desulfovibrio gigas. This protein presents a region where backbone amide protons exchange fast with bulk solvent becoming undetectable. These residues were assigned using C-13-detection experiments.},
	doi = {10.1007/s12104-007-9022-3},
	author = {Pauleta, Sofia R and Duarte, Americo G and Carepo, Marta S and Pereira, Alice S. and Tavares, Pedro and Moura, Isabel and Moura, Jose J. G.}
}
@article {Pereira:1998tv,
	title = {{Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization}},
	journal = {Biochemistry},
	volume = {37},
	number = {28},
	year = {1998},
	note = {101XQ
Times Cited:75
Cited References Count:42},
	pages = {9871{\textendash}9876},
	abstract = {Rapid freeze-quench (RFQ) Mossbauer and stopped-flow absorption spectroscopy were used to monitor the ferritin ferroxidase reaction using recombinant (apo) frog M ferritin; the initial transient ferric species could be trapped by the RFQ method using low iron loading (36 Fe2+/ferritin molecule). Biphasic kinetics of ferroxidation were observed and measured directly by the Mossbauer method; a majority (85\%) of the ferrous ions was oxidized at a fast rate of similar to 80 s(-1) and the remainder at a much slower rate of similar to 1.7 s(-1). In parallel with the fast phase oxidation of the Fe2+ ions, a single transient iron species is formed which exhibits magnetic properties (diamagnetic ground state) and Mossbauer parameters (Delta E-Q = 1.08 +/- 0.03 mm/s and delta = 0.62 +/- 0.02 mm/s) indicative of an antiferromagnetically coupled peroxodiferric complex. The formation and decay rates of this transient diiron species measured by the RFQ Mossbauer method match those of a transient blue species (lambda(max) = 650 nm) determined by the stopped-flow absorbance measurement. Thus, the transient colored species is assigned to the same peroxodiferric intermediate. Similar transient colored species have been detected by other investigators in several other fast ferritins (H and M subunit types), such as the human H ferritin and the Escherichia coli ferritin, suggesting a similar mechanism for the ferritin ferroxidase step in all fast ferritins. Peroxodiferric complexes are also formed as early intermediates in the reaction of O-2 With the catalytic diiron centers in the hydroxylase component of soluble methane monooxygenase (MMOH) and in the D84E mutant of the R2 subunit of E. coli ribonucleotide reductase. The proposal that a single protein site, with a structure homologous to the diiron centers in MMOH and R2, is involved in the ferritin ferroxidation step is confirmed by the observed kinetics, spectroscopic properties, and purity of the initial peroxodiferric species formed in the frog M ferritin.},
	author = {Pereira, A. and Small, W and Krebs, C and Tavares, P. and Edmondson, D and Theil, E and Huynh, B}
}
@article {Pereira:1997ws,
	title = {{Rapid and parallel formation of Fe3+ multimers, including a trimer, during H-type subunit ferritin mineralization}},
	journal = {Biochemistry},
	volume = {36},
	number = {25},
	year = {1997},
	note = {Xg901
Times Cited:25
Cited References Count:53},
	month = {jun},
	pages = {7917{\textendash}7927},
	abstract = {Conversion of Fe ions in solution to the solid phase in ferritin concentrates iron required for cell function. The rate of the Fe phase transition in ferritin is tissue specific and reflects the differential expression of two classes of ferritin subunits (H and L). Early stages of mineralization were probed by rapid freeze-quench Mossbauer, at strong fields (up to 8 T), and EPR spectroscopy in an H-type subunit, recombinant frog ferritin; small numbers of Fe (36 moles/mol of protein) were used to increase Fe3+ in mineral precursor forms, At 25 ms, four Fe3+-oxy species (three Fe dimers and one Fe trimer) were identified, These Fe3+-oxy species were found to form at similar rates and decay subsequently to a distinctive superparamagentic species designated the {\textquoteright}{\textquoteright}young core.{\textquoteright}{\textquoteright} The rate of oxidation of Fe2+ (1026 s(-1)) corresponded well to the formation constant for the Fe3+- tyrosinate complex (920 s(-1)) observed previously [Waldo, G. S., {\&} Theil, E. C. (1993) Biochemistry 32, 13261] and, coupled with EPR data, indicates that several or possibly all of the Fe3+-oxy species involve tyrosine. The results, combined with previous Mossbauer studies of Y30F human H-type ferritin which showed decreases in several Fe3+ intermediates and stabilization of Fe2+ [Bauminger, E. R., et al. (1993) Biochem, J. 296, 709], emphasize the involvement of tyrosyl residues in the mineralization of H-type ferritins. The subsequent decay of these multiple Fe3+-oxy species to the superparamagnetic mineral suggests that Fe3+ species in different environments may be translocated as intact units from the protein shell into the ferritin cavity where the conversion to a solid mineral occurs.},
	author = {Pereira, A. and Tavares, P. and Lloyd, S and Danger, D and Edmondson, D and Theil, E and Huynh, B}
}
@article {Pereira:1999vu,
	title = {{Biochemical and spectroscopic characterization of overexpressed fuscoredoxin from Escherichia coli}},
	journal = {Biochemical And Biophysical Research Communications},
	volume = {260},
	number = {1},
	year = {1999},
	pages = {209{\textendash}215},
	abstract = {Fuscoredoxin is a unique iron containing protein of yet unknown function originally discovered in the sulfate reducers of the genus Desulfovibrio. It contains two iron-sulfur clusters: a cubane [4Fe-4S] and a mixed oxo- and sulfide-bridged 4Fe cluster of unprecedented structure. The recent determination of the genomic sequence of Escherichia coli (E. coli) has revealed a homologue of fuscoredoxin in this facultative microbe. The presence of this gene in E. coli raises interesting questions regarding the function of fuscoredoxin and whether this gene represents a structural homologue of the better-characterized Desulfovibrio proteins. In order to explore the latter, an overexpression system for the E. coli fuscoredoxin gene was devised. The gene was cloned from genomic DNA by use of the polymerase chain reaction into the expression vector pT7-7 and overexpressed in E. coli BL21(DE3) cells. After two chromatographic steps a good yield of recombinant protein was obtained (approximately 4 mg of pure protein per liter of culture). The purified protein exhibits an optical spectrum characteristic of the homologue from D. desulfuricans, indicating that cofactor assembly was accomplished. Iron analysis indicated that the protein contains circa 8 iron atoms/molecule which were shown by EPR and Mossbauer spectroscopies to be present as two multinuclear clusters, albeit with slightly altered spectroscopic features. A comparison of the primary sequences of fuscoredoxins is presented and differences on cluster coordination modes are discussed on the light of the spectroscopic data. (C) 1999 Academic Press.},
	author = {Pereira, AS and Tavares, P. and Krebs, C and HUYNH, BH and Rusnak, F and Moura, I and Moura, JJG}
}
@article {Pereira:2001ic,
	title = {{Mossbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase}},
	journal = {Journal Of The American Chemical Society},
	volume = {123},
	number = {12},
	year = {2001},
	pages = {2771{\textendash}2782},
	abstract = {The periplasmic hydrogenase of Desulfovibrio vulgaris (Hildenbourough) is an all Fe-containing hydrogenase. It contains two ferredoxin type [4Fe-4S] clusters, termed the F clusters, and a catalytic H cluster. Recent X-ray crystallographic studies on two Fe hydrogenases revealed that the H cluster is composed of two sub-clusters, a [4Fe-4S] cluster ([4Fe-4S]H) and-a binuclear Fe cluster ([2Fe]H), bridged by a cysteine sulfur. The aerobically purified D. vulgaris hydrogenase is stable in air. It is inactive and requires reductive activation. Upon reduction, the enzyme becomes sensitive to O-2 indicating that the reductive activation process is irreversible. Previous EPR investigations showed that upon reoxidation (under argon) the H cluster exhibits a rhombic EPR signal that is not seen in the as-purified enzyme, suggesting a conformational change in association with the reductive activation. For the purpose of gaining more information on the electronic properties of this unique H cluster and to understand further the reductive activation process, variable-temperature and variable-field Mossbauer spectroscopy has been used to characterize the Fe-S clusters in D. vulgaris hydrogenase poised at different redox states generated during a reductive titration, and in the GO-reacted enzyme. The data were successfully decomposed into spectral components corresponding to the F and H clusters,and characteristic parameters describing the electronic and magnetic properties of the F and H clusters were obtained. Consistent with the X-ray crystallographic results, the spectra of the H cluster can be understood as originating from an exchange coupled [4Fe-4S] - [2Fe] system. In particular, detailed analysis of the data reveals that the reductive activation begins with reduction of the [4Fe-4S]H cluster from the 2+ to the If state, followed by transfer of the reducing equivalent from the [4Fe-4S]H subcluster to the binuclear [2Fe]H subcluster. The results also reveal that binding of exogenous CO to the H cluster affects significantly the exchange coupling between the [4Fe-4S]H and the [2Fe]H subclusters. Implication of such a CO binding effect is discussed.},
	doi = {10.1021/ja003176+},
	author = {Pereira, AS and Tavares, P. and Moura, I and Moura, JJG and HUYNH, BH}
}
@article {Pereira:2007tu,
	title = {{Superoxide reductases}},
	journal = {European Journal of Inorganic Chemistry},
	number = {18},
	year = {2007},
	note = {188RP
Times Cited:2
Cited References Count:97},
	month = {jun},
	pages = {2569{\textendash}2581},
	abstract = {Reactive oxygen species (ROS), when in excess, are among the most deleterious species an organism can deal with. The physiological effects of ROS include amino acid chain cleavage, DNA degradation and lipid oxidation, among others. They can be formed in the cytoplasm in a variety of ways, including autooxidation reactions (FMN- and FAD-containing enzymes) and Fenton reactions as a result of the cytoplasmatic pool of iron ions. The superoxide anion (021, despite its short half-life in solution, is particularly pernicious as it can form other reactive ROS (such as the strong oxidant peroxynitrite) or oxidize and/or reduce cellular components. For strict anaerobic or microaerophilic bacteria it is of particular importance to be able to dispose of ROS in a controlled manner, especially if these organisms are temporarily exposed to air. This review aims to describe the structural characteristics of superoxide reductases (SORs) and mechanistic aspects of biological superoxide anion reduction. SORs can be considered the main class of enzymes behind the oxygen detoxification pathway of anaerobic and microaerophilic bacteria. The geometry of the active site (three classes have been described), the possible electron donors in vivo and the current hypothesis for the catalytic mechanism will be discussed. Some phylogenetic considerations are presented, regarding the primary structure of SORs currently available in genome databases. ((c) Wiley-VCH Verlag GmbH {\&} Co. KGaA, 69451 Weinheim, Germany, 2007).},
	author = {Pereira, A. and Tavares, P. and Folgosa, F and Almeida, R and Moura, I and Moura, J}
}
@article {Prudencio:1999ud,
	title = {{Copper-containing nitrous oxide reductase from Pseudomonas nautica: spectroscopic and redox properties}},
	journal = {Journal Of Inorganic Biochemistry},
	volume = {74},
	number = {1-4},
	year = {1999},
	pages = {267{\textendash}267},
	author = {Prudencio, M and Pereira, AS and Tavares, P. and Besson, S and Moura, I}
}
@article {Prudencio:2000wl,
	title = {{Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617}},
	journal = {Biochemistry},
	volume = {39},
	number = {14},
	year = {2000},
	pages = {3899{\textendash}3907},
	author = {Prudencio, M and Pereira, A. and Tavares, P. and Besson, S and Cabrito, I and Brown, K and Samyn, B and Devreese, B and VanBeeumen, J and Rusnak, F and Fauque, G and Moura, J and Tegoni, M and Cambillau, C and Moura, I}
}
