@article {Gavel:2008fx,
	title = {{A new type of metal-binding site in cobalt- and zinc-containing adenylate kinases isolated from sulfate-reducers Desulfovibrio gigas and Desulfovibrio desulfuricans ATCC 27774}},
	journal = {Journal Of Inorganic Biochemistry},
	volume = {102},
	number = {5-6},
	year = {2008},
	pages = {1380{\textendash}1395},
	abstract = {Adenylate kinase (AK) mediates the reversible transfer of phosphate groups between the adenylate nucleotides and contributes to the maintenance of their constant cellular level, necessary for energy metabolism and nucleic acid synthesis. The AK were purified from crude extracts of two sulfate-reducing bacteria (SRB), Desulfovibrio (D.) gigas NCIB 9332 and Desulfovibrio desulfuricans ATCC 27774, and biochemically and spectroscopically characterised in the native and fully cobalt- or zinc-substituted forms. These are the first reported adenylate kinases that bind either zinc or cobalt and are related to the subgroup of metal-containing AK found, in most cases, in Gram-positive bacteria. The electronic absorption spectrum is consistent with tetrahedral coordinated cobalt, predominantly via sulfur ligands, and is supported by EPR. The involvement of three cysteines in cobalt or zinc coordination was confirmed by chemical methods. Extended X-ray absorption fine structure (EXAFS) indicate that cobalt or zinc are bound by three cysteine residues and one histidine in the metal-binding site of the "LID" domain. The sequence (129)Cys-X-5-His-X-15-Cys-X-2-Cys of the AK from D. gigas is involved in metal coordination and represents a new type of binding motif that differs from other known zinc-binding sites of AK. Cobalt and zinc play a structural role in stabilizing the LID domain. (C) 2008 Elsevier Inc. All rights reserved.},
	doi = {10.1016/j.jinorgbio.2008.01.023},
	author = {Gavel, Olga Yu and Bursakov, Sergey A. and Di Rocco, Giulia and Trincao, Jose and Pickering, Ingrid J. and George, Graham N. and Calvete, Juan J. and Shnyrov, Valery L. and Brondino, Carlos D. and Pereira, Alice S. and Lampreia, Jorge and Tavares, Pedro and Moura, Jose J. G. and Moura, Isabel}
}
@article {Auchere:2003um,
	title = {{Formation of a stable cyano-bridged dinuclear iron cluster following oxidation of the superoxide reductases from Treponema pallidum and Desulfovibrio vulgaris with K(3)Fe(CN)(6)}},
	journal = {Inorganic chemistry},
	volume = {42},
	number = {4},
	year = {2003},
	note = {0020-1669 (Print)
Journal Article},
	pages = {938{\textendash}940},
	abstract = {Superoxide reductases catalyze the monovalent reduction of superoxide anion to hydrogen peroxide. Spectroscopic evidence for the formation of a dinuclear cyano-bridged adduct after K(3)Fe(CN)(6) oxidation of the superoxide reductases neelaredoxin from Treponema pallidum and desulfoferrodoxin from Desulfovibrio vulgaris was reported. Oxidation with K(3)Fe(CN)(6) reveals a band in the near-IR with lambda(max) at 1020 nm, coupled with an increase of the iron content by almost 2-fold. Fourier transform infrared spectroscopy provided additional evidence with CN-stretching vibrations at 2095, 2025-2030, and 2047 cm(-)(1), assigned to a ferrocyanide adduct of the enzyme. Interestingly, the low-temperature electronic paramagnetic resonance (EPR) spectra of oxidized TpNlr reveal at least three different species indicating structural heterogeneity in the coordination environment of the active site Fe ion. Given the likely 6-coordinate geometry of the active site Fe(3+) ion in the ferrocyanide adduct, we propose that the rhombic EPR species can serve as a model of a hexacoordinate form of the active site.},
	author = {Auchere, F and Raleiras, P and Benson, L and Venyaminov, S and Tavares, P. and Moura, J and Moura, I and Rusnak, F}
}
@article {Cabrito:2001tc,
	title = {{Nitrous oxide reductase (N2OR) from Pseudomonas nautica 617}},
	journal = {Journal Of Inorganic Biochemistry},
	volume = {86},
	number = {1},
	year = {2001},
	pages = {165{\textendash}165},
	author = {Cabrito, I and Pereira, AS and Tavares, P. and Besson, S and Brondino, C and Hoffman, B and Brown, K and Tegoni, M and Cambillau, C and Moura, JJG and Moura, I}
}
@article {Franco:2001ur,
	title = {{Substitution of murine ferrochelatase glutamate-287 with glutamine or alanine leads to porphyrin substrate-bound variants}},
	journal = {Biochemical Journal},
	volume = {356},
	year = {2001},
	pages = {217{\textendash}222},
	abstract = {Ferrochelatase (EC 4.99.1.1) is the terminal enzyme of the haem biosynthetic pathway and catalyses iron chelation into the protoporphyrin IX ring. Glutamate-287 (E287) of murine mature ferrochelatase is a conserved residue in all known sequences of ferrochelatase, is present at the active site of the enzyme, as inferred from the Bacillus subtilis ferrochelatase three-dimensional structure, and is critical for enzyme activity. Substitution of E287 with either glutamine (Q) or alanine (A) yielded variants with lower enzymic activity than that of the wild-type ferrochelatase and with different absorption spectra from the wild-type enzyme. In contrast to the wild-type enzyme, the absorption spectra of the variants indicate that these enzymes, as purified, contain protoporphyrin IX. Identification and quantification of the porphyrin bound to the E287-directed variants indicate that approx. 80\% of the total porphyrin corresponds to protoporphyrin IX. Significantly, rapid stopped-flow experiments of the E287A and E287Q Variants demonstrate that reaction with Zn2+ results in the formation of bound Zn-protoporphyrin IX, indicating that the endogenously bound protoporphyrin IX can be used as a substrate. Taken together, these findings suggest that the structural strain imposed by ferrochelatase on the porphyrin substrate as a critical step in the enzyme catalytic mechanism is also accomplished by the E287A and E287Q variants, but without the release of the product. Thus E287 in murine ferrochelatase appears to be critical For the catalytic process by controlling the release of the product.},
	author = {Franco, R and Pereira, AS and Tavares, P. and Mangravita, A and Barber, MJ and Moura, I and Ferreira, GC}
}
@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}
}
@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 {Almendra:1999uy,
	title = {{Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas}},
	journal = {Biochemistry},
	volume = {38},
	number = {49},
	year = {1999},
	pages = {16366{\textendash}16372},
	abstract = {An air-stable formate dehydrogenase (FDH), an enzyme that catalyzes the oxidation of formate to carbon dioxide, was purified from the sulfate reducing organism Desulfovibrio gigas (D. gigas) NCIB 9332. D. gigas FDH is a heterodimeric protein [alpha (92 kDa) and beta (29 kDa) subunits] and contains 7 +/- 1 Fe/protein and 0.9 +/- 0.1 W/protein, Selenium was not detected. The UV/visible absorption spectrum of D, gigas FDH is typical of an iron-sulfur protein. Analysis of pterin nucleotides yielded a content of 1.3 +/- 0.1 guanine monophosphate/mol of enzyme, which suggests a tungsten coordination with two molybdopterin guanine dinucleotide cofactors. Both Mossbauer spectroscopy performed on D. gigas FDH grown in a medium enriched with Fe-57 and EPR studies performed in the native and fully reduced state of the protein confirmed the presence of two [4Fe-4S] clusters. Variable-temperature EPR studies showed the presence of two signals compatible with an atom in a d(1) configuration albeit with an unusual relaxation behavior as compared to the one generally observed for W(V) ions.},
	author = {Almendra, MJ and Brondino, CD and Gavel, O and Pereira, AS and Tavares, P. and Bursakov, S and Duarte, R and CALDEIRA, J and Moura, JJG and Moura, I}
}
