@article { ISI:000260837700013,
	title = {Biochemical and spectroscopic characterization of the membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617},
	journal = {JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY},
	volume = {13},
	number = {8},
	year = {2008},
	month = {NOV},
	pages = {1321-1333},
	abstract = {Membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617 can be solubilized in either of two ways that will ultimately determine the presence or absence of the small (I) subunit. The enzyme complex (NarGHI) is composed of three subunits with molecular masses of 130, 65, and 20 kDa. This enzyme contains approximately 14 Fe, 0.8 Mo, and 1.3 molybdopterin guanine dinucleotides per enzyme molecule. Curiously, one heme b and 0.4 heme c per enzyme molecule have been detected. These hemes were potentiometrically characterized by optical spectroscopy at pH 7.6 and two noninteracting species were identified with respective midpoint potentials at E(m) = + 197 mV (heme c) and-4.5 mV (heme b). Variable-temperature (4-120 K) X-band electron paramagnetic resonance (EPR) studies performed on both as-isolated and dithionite-reduced nitrate reductase showed, respectively, an EPR signal characteristic of a {[}3Fe-4S](+) cluster and overlapping signals associated with at least three types of {[}4Fe-4S](+) centers. EPR of the as-isolated enzyme shows two distinct pH-dependent Mo(V) signals with hyperfine coupling to a solvent-exchangeable proton. These signals, called {\textquoteleft}{\textquoteleft}lowpH{\textquoteright}{\textquoteright} and {\textquoteleft}{\textquoteleft}high-pH,{\textquoteright}{\textquoteright} changed to a pH-independent Mo(V) signal upon nitrate or nitrite addition. Nitrate addition to dithionite-reduced samples at pH 6 and 7.6 yields some of the EPR signals described above and a new rhombic signal that has no hyperfine structure. The relationship between the distinct EPR-active Mo(V) species and their plausible structures is discussed on the basis of the structural information available to date for closely related membrane-bound nitrate reductases.},
	issn = {0949-8257},
	doi = {10.1007/s00775-008-0416-1},
	author = {Correia, Cristina and Besson, Stephane and Brondino, Carlos D. and Gonzalez, Pablo J. and Fauque, Guy and Lampreia, Jorge and Moura, Isabel and Moura, Jose J. G.}
}
@article { ISI:000256239600042,
	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},
	note = {13th International Conference on Biological Inorganic Chemistry, Vienna, AUSTRIA, JUL 15-20, 2007},
	month = {MAY-JUN},
	pages = {1380-1395},
	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 {\textquoteleft}{\textquoteleft}LID{{\textquoteright}{\textquoteright}} 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.},
	issn = {0162-0134},
	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 { ISI:000247904400005,
	title = {Crystal structure of the 16 heme cytochrome from Desulfovibrio gigas: A glycosylated protein in a sulphate-reducing bacterium},
	journal = {JOURNAL OF MOLECULAR BIOLOGY},
	volume = {370},
	number = {4},
	year = {2007},
	month = {JUL 20},
	pages = {659-673},
	abstract = {Sulphate-reducing bacteria have a wide variety of periplasmic cytochromes involved in electron transfer from the periplasm to the cytoplasm. HmcA is a high molecular mass cytochrome of 550 amino acid residues that harbours 16 c-type heme groups. We report the crystal structure of HmcA isolated from the periplasm of Desulfovibrio gigas. Crystals were grown. using polyethylene glycol 8K and zinc acetate, and diffracted beyond 2.1 angstrom resolution. A multiple-wavelength anomalous dispersion experiment at the iron absorption edge enabled us to obtain good-quality phases for structure solution and model building. DgHmcA has a V-shape architecture, already observed in HmcA isolated from Desulfovibrio vulgaris Hildenborough. The presence of an oligosaccharide molecule covalently bound to an Asn residue was observed in the electron density maps of DgHmcA and confirmed by mass spectrometry. Three modified monosaccharides appear at the highly hydrophobic vertex, possibly acting as an anchor of the protein to the cytoplasmic membrane. (c) 2007 Elsevier Ltd. All rights reserved.},
	issn = {0022-2836},
	doi = {10.1016/j.jmb.2007.04.055},
	author = {Santos-Silva, Teresa and Dias, Joao Miguel and Dolla, Alain and Durand, Marie-Claire and Goncalves, Luisa L. and Lampreia, Jorge and Moura, Isabel and Romao, Maria Joao}
}
@article { ISI:000221678300020,
	title = {Antagonists Mo and Cu in a heterometallic cluster present on a novel protein (orange protein) isolated from Desulfovibrio gigas},
	journal = {JOURNAL OF INORGANIC BIOCHEMISTRY},
	volume = {98},
	number = {5},
	year = {2004},
	note = {11th International Conference on Biological Inorganic Chemistry, Cairns, AUSTRALIA, JUL 19-23, 2003},
	month = {MAY},
	pages = {833-840},
	abstract = {An orange-coloured protein (ORP) isolated from Desulfovibrio gigas, a sulphate reducer, has been previously shown by extended X-ray absorption fine structure (EXAFS) to contain a novel mixed-metal sulphide cluster of the type {[}S2MoS2CuS2MoS2] {[}J. Am. Chem. Soc. 122 (2000) 8321]. We report here the purification and the biochemical/spectroscopic characterisation of this novel protein. ORP is a soluble monomeric protein (11.8 kDa). The cluster is non-covalently bound to the polypeptide chain. The presence of a MoS42- moiety in the structure of the cofactor contributes with a quite characteristic UV-Vis spectra, exhibiting an orange colour, with intense absorption peaks at 480 and 338 nm. Pure ORP reveals an Abs(480)/Abs(338) ratio of 0.535. The gene sequence coding for ORP as well as the amino acid sequence was determined. The putative biological function of ORP is discussed. (C) 2003 Elsevier Inc. All rights reserved.},
	issn = {0162-0134},
	doi = {10.1016/j.jinorgbio.2003.12.002},
	author = {Bursakov, SA and Gavel, OY and Di Rocco, G and Lampreia, J and Calvete, J and Pereira, AS and Moura, JJG and Moura, I}
}
@article { ISI:000185370100005,
	title = {The isolation and characterization of cytochrome c nitrite reductase subunits (NrfA and NrfH) from Desulfovibrio desulfuricans ATCC 27774 - Re-evaluation of the spectroscopic data and redox properties},
	journal = {EUROPEAN JOURNAL OF BIOCHEMISTRY},
	volume = {270},
	number = {19},
	year = {2003},
	month = {OCT},
	pages = {3904-3915},
	abstract = {The cytochrome c nitrite reductase is isolated from the membranes of the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 as a heterooligomeric complex composed by two subunits (61 kDa and 19 kDa) containing c-type hemes, encoded by the genes nrfA and nrfH, respectively. The extracted complex has in average a 2NrfA:1NrfH composition. The separation of ccNiR subunits from one another is accomplished by gel filtration chromatography in the presence of SDS. The amino-acid sequence and biochemical subunits characterization show that NrfA contains five hemes and NrfH four hemes. These considerations enabled the revision of a vast amount of existing spectroscopic data on the NrfHA complex that was not originally well interpreted due to the lack of knowledge on the heme content and the oligomeric enzyme status. Based on EPR and Mossbauer parameters and their correlation to structural information recently obtained from X-ray crystallography on the NrfA structure {[}Cunha, C. A., Macieira, S., Dias, J.M., Almeida, M.G., Goncalves, L. M. L., Costa, C., Lampreia, J., Huber, R., Moura, J. J. G., Moura, I. \& Romano, M. (2003) J. Biol. Chem. 278, 17455-17465], we propose the full assignment of midpoint reduction potentials values to the individual hemes. NrfA contains the high-spin catalytic site (-80 mV) as well as a quite unusual high reduction potential (+150 mV)/low-spin bis-His coordinated heme, considered to be the site where electrons enter. In addition, the reassessment of the spectroscopic data allowed the first partial spectroscopic characterization of the NrfH subunit. The four NrfH hemes are all in a low-spin state (S = 1/2). One of them has a g(max) at 3.55, characteristic of bis-histidinyl iron ligands in a noncoplanar arrangement, and has a positive reduction potential.},
	issn = {0014-2956},
	doi = {10.1046/j.1432-1033.2003.03772.x},
	author = {Almeida, MG and Macieira, S and Goncalves, LL and Huber, R and Cunha, CA and Romao, MJ and Costa, C and Lampreia, J and Moura, JJG and Moura, I}
}
@article { ISI:000182818600133,
	title = {Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 - The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA)},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {278},
	number = {19},
	year = {2003},
	month = {MAY 9},
	pages = {17455-17465},
	abstract = {The gene encoding cytochrome c nitrite reductase (NrfA) from Desulfovibrio desulfuricans ATCC 27774 was sequenced and the crystal structure of the enzyme was determined to 2.3-Angstrom resolution. In comparison with homologous structures, it presents structural differences mainly located at the regions surrounding the putative substrate inlet and product outlet, and includes a well defined second calcium site with octahedral geometry, coordinated to propionates of hemes 3 and 4, and caged by a loop non-existent in the previous structures. The highly negative electrostatic potential in the environment around hemes 3 and 4 suggests that the main role of this calcium ion may not be electrostatic but structural, namely in the stabilization of the conformation of the additional loop that cages it and influences the solvent accessibility of heme 4. The NrfA active site is similar to that of peroxidases with a nearby calcium site at the heme distal side nearly in the same location as occurs in the class II and class III peroxidases. This fact suggests that the calcium ion at the distal side of the active site in the NrfA enzymes may have a similar physiological role to that reported for the peroxidases.},
	issn = {0021-9258},
	doi = {10.1074/jbc.M211777200},
	author = {Cunha, CA and Macieira, S and Dias, JM and Almeida, G and Goncalves, LL and Costa, C and Lampreia, J and Huber, R and Moura, JJG and Moura, I and Romao, MJ}
}
@article { ISI:000170467300379,
	title = {Cloning of a novel Mo-Cu containing protein from Desulfovibrio.gigas},
	journal = {JOURNAL OF INORGANIC BIOCHEMISTRY},
	volume = {86},
	number = {1},
	year = {2001},
	month = {AUG},
	pages = {202},
	issn = {0162-0134},
	author = {Di Rocco, G and Pereira, AS and Bursakov, SA and Gavel, OY and Rusnak, F and Lampreia, J and Moura, JJG and Moura, I}
}
@article { ISI:000170467300301,
	title = {Cobalt/Zinc as structural elements of bacterial adenylate kinase},
	journal = {JOURNAL OF INORGANIC BIOCHEMISTRY},
	volume = {86},
	number = {1},
	year = {2001},
	month = {AUG},
	pages = {163},
	issn = {0162-0134},
	author = {Bursakov, SA and Gavel, OY and Di Rocco, G and Lampreia, J and Shnyrov, VL and George, GN and Calvete, JJ and Moura, JJG and Moura, I}
}
@article { ISI:000170467300216,
	title = {Developmen of an electrochemical biosensor for nitrite determination},
	journal = {JOURNAL OF INORGANIC BIOCHEMISTRY},
	volume = {86},
	number = {1},
	year = {2001},
	month = {AUG},
	pages = {121},
	issn = {0162-0134},
	author = {Almeida, G and Tavares, P. and Lampreia, J and Moura, JJG and Moura, I}
}
@article { ISI:000170467300346,
	title = {Spectroscopic characterization of the membrane nitrate reductase isolated from Pseudomonas nautica},
	journal = {JOURNAL OF INORGANIC BIOCHEMISTRY},
	volume = {86},
	number = {1},
	year = {2001},
	month = {AUG},
	pages = {186},
	issn = {0162-0134},
	author = {Correia, C and Carneiro, C and Besson, S and Fauque, G and Lampreia, J and Moura, I and Moura, JJG}
}
@article { ISI:000170467300603,
	title = {Structural studies on Desulfovibrio desulfuricans ATCC 27774 multiheme nitrite reductase - characterization of the subunits},
	journal = {JOURNAL OF INORGANIC BIOCHEMISTRY},
	volume = {86},
	number = {1},
	year = {2001},
	month = {AUG},
	pages = {316},
	issn = {0162-0134},
	author = {Goncalves, LML and Cunha, C and Almeida, G and Macieira, S and Costa, C and Lampreia, J and Romao, MJ and Moura, JJG and Moura, I}
}
@article { ISI:000085557600020,
	title = {Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774},
	journal = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY},
	volume = {56},
	number = {Part 2},
	year = {2000},
	month = {FEB},
	pages = {215-217},
	abstract = {{Nitrite reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is a multihaem (type c) membrane-bound enzyme that catalyzes the dissimilatory conversion of nitrite to ammonia. Crystals of the oxidized form of this enzyme were obtained using PEG and CaCl2 as precipitants in the presence of 3-(decylmethylammonium)propane-1-sulfonate and belong to the space group P2(1)2(1)2(1), With unit-cell parameters a = 78.94},
	issn = {0907-4449},
	doi = {10.1107/S0907444999016066},
	author = {Dias, JM and Cunha, CA and Teixeira, S and Almeida, G and Costa, C and Lampreia, J and Moura, JJG and Moura, I and Romao, MJ}
}
@article { ISI:000079238200022,
	title = {Cross-linking between cytochrome c(3) and flavodoxin from Desulfovibrio gigas},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {256},
	number = {2},
	year = {1999},
	month = {MAR 16},
	pages = {367-371},
	abstract = {Tetraheme cytochrome c(3) (13 kDa) and flavodoxin (16 kDa), are small electron transfer proteins that have been used to mimic, in vitro, part of the electron-transfer chain that operates between substract electron donors and respiratory electron accepters partners in Desulfovibrio species (Palma, N., Moura, I., LeGall, J., Van Beeumen, J., Wampler, J., Moura, J. J. G. (1994) Biochemistry 33, 6394-6407). The electron transfer between these two proteins is believed to occur through the formation of a specific complex where electrostatic interaction is the main driving force (Stewart, D., LeGall, J., Moura, I., Moura, J.J.G., Peck, H.D., Xavier, A.V., Weiner, P.K. and Wampler, J.E. (1988) Biochemistry 27, 2444-2450, Stewart, D., LeGall, J., Moura, I., Moura, J.J.G., Peck, H.D., Xavier, A.V., Weiner, P., Wampler, J. (1989) fur. J. Biochem. 185, 695-700). In order to obtain structural information of the pre-complex, a covalent complex between the two proteins was prepared. A water-soluble carbodiimide {[}EDC (1-ethyl-3(3 dimethylaminopropyl) carbodiimide hydrochloride] was used for the cross linking reaction. The reaction was optimized varying a wide number of experimental parameters such as ionic strength, protein and cross linker concentration, and utilization of different cross linkers and reaction time between the crosslinker and proteins. (C) 1999 Academic Press.},
	issn = {0006-291X},
	doi = {10.1006/bbrc.1999.0201},
	author = {Correia, C and Monzani, E and Moura, I and Lampreia, J and Moura, JJG}
}
@article { ISI:000081157700113,
	title = {New biochemical studies on nitrite reductase from Desulfovibrio desulfuricans ATCC 27774},
	journal = {JOURNAL OF INORGANIC BIOCHEMISTRY},
	volume = {74},
	number = {1-4},
	year = {1999},
	month = {APR 30},
	pages = {63},
	issn = {0162-0134},
	author = {Almeida, G and Lampreia, J and Moura, JJG and Moura, I}
}
@article { ISI:000073305602620,
	title = {Myofibrillar and sarcoplasmic proteins and cathepsin D activity},
	journal = {FASEB JOURNAL},
	volume = {11},
	number = {9, S},
	year = {1997},
	month = {JUL 31},
	pages = {2134},
	issn = {0892-6638},
	author = {Correia, JHRD and Lampreia, J and Matta, A and Mateus, C and Prates, J and Rosa, J and Correia, M and Correia, AD and Peixoto, C}
}
@article { ISI:000073305602622,
	title = {Myofibrillar proteins and cathepsin D activity during different technologies and variations with time},
	journal = {FASEB JOURNAL},
	volume = {11},
	number = {9, S},
	year = {1997},
	month = {JUL 31},
	pages = {2133},
	issn = {0892-6638},
	author = {Correia, AD and Correia, JHRD and Prates, J and Mateus, C and Matta, A and Rosa, J and Correia, M and Lampreia, J and Peixoto, C}
}
@article { ISI:A1996VW61600025,
	title = {Preliminary crystallographic analysis and further characterization of a dodecaheme cytochrome c from Desulfovibrio desulfuricans ATCC 27774},
	journal = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY},
	volume = {52},
	number = {Part 6},
	year = {1996},
	month = {NOV 1},
	pages = {1202-1208},
	abstract = {{Dodecaheme cytochrome c has been purified from Desulfovibrio (D.) desulfuricans ATCC 27774 cells grown under both nitrate and sulfate-respiring conditions. Therefore, it is likely to play a role in the electron-transfer system of both respiratory chains. Its molecular mass (37 768 kDa) was determined by electrospray mass spectrometry. Its first 39 amino acids were sequenced and a motif was found between amino acids 32 and 37 that seems to exist in all the cytochromes of the c3 type from sulfate-reducing bacteria sequenced at present. The midpoint redox potentials of this cytochrome were estimated to be -68, -120, -248 and -310 mV. Electron paramagnetic resonance spectroscopy of the oxidized cytochrome shows several low-spin components with a g(max) spreading from 3.254 to 2.983. Two crystalline forms were obtained by vapour diffusion from a solution containing 2\% PEG 6000 and 0.25-0.75 M acetate buffer pH = 5.5. Both crystals belong to monoclinic space groups: one is PZ,, with a = 61.00},
	issn = {0907-4449},
	doi = {10.1107/S090744499600738X},
	author = {Coelho, AV and Matias, PM and Sieker, LC and Morais, J and Carrondo, MA and Lampreia, J and Costa, C and Moura, JJG and Moura, I and LeGall, J}
}
@article { ISI:A1996UK22800002,
	title = {Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins},
	journal = {FEBS LETTERS},
	volume = {385},
	number = {3},
	year = {1996},
	month = {MAY 6},
	pages = {138-142},
	abstract = {The primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a redox protein with two mononuclear iron sites, was determined by automatic Edman degradation and mass spectrometry of the composing peptides, It contains 125 amino acid residues of which five are cysteines, The first four, Cys-9, Cys-12, Cys-28 and Cys-29, are responsible for the binding of Center I which has a distorted tetrahedral sulfur coordination similar to that found in desulforedoxin from D. gigas, The remaining Cys-115 is proposed to be involved in the coordination of Center II, which is probably octahedrally coordinated with predominantly nitrogen/oxygen containing ligands as previously suggested by Mossbauer and Raman spectroscopy.},
	issn = {0014-5793},
	doi = {10.1016/0014-5793(96)00364-X},
	author = {Devreese, B and Tavares, P. and Lampreia, J and VanDamme, N and LeGall, J and Moura, JJG and VanBeeumen, J and Moura, I}
}
@article { ISI:A1996UF91100036,
	title = {Characterization of representative enzymes from a sulfate reducing bacterium implicated in the corrosion of steel},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {221},
	number = {2},
	year = {1996},
	month = {APR 16},
	pages = {414-421},
	abstract = {This communication reports the isolation, purification and characterization of key enzymes involved in dissimilatory sulfate reduction of a sulfate reducing bacterium classified as Desulfovibrio desulfuricans subspecies desulfuricans New Jersey (NCIMB 8313) (Ddd NJ). The chosen strain, originally recovered from a corroding cast iron heat exchanger, was grown in large scale batch cultures. Physico-chemical and spectroscopic studies of the purified enzymes were carried out. These analyses revealed a high degree of similarity between proteins isolated from the DddNJ strain and the homologous proteins obtained from Desulfomicrobium baculatus Norway 4. In view of the results obtained, taxonomic reclassification of Desulfovibrio desulfuricans subspecies desulfuricans New Jersey (NCIMB 8313) into Desulfomicrobium baculatus (New Jersey) is proposed. (C) 1996 Academic Press, Inc.},
	issn = {0006-291X},
	doi = {10.1006/bbrc.1996.0610},
	author = {Pereira, AS and Franco, R and Feio, MJ and Pinto, C and Lampreia, J and Reis, MA and Calvete, J and Moura, I and Beech, I and Lino, AR and Moura, JJG}
}
@article { ISI:A1995RA25300017,
	title = {SPROUT - 3D STRUCTURE GENERATION USING TEMPLATES},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND COMPUTER SCIENCES},
	volume = {35},
	number = {3},
	year = {1995},
	month = {MAY-JUN},
	pages = {479-493},
	abstract = {SPROUT is a computer program for the rational design of molecules for a range of applications in molecular recognition. Molecular graphs are built in a stepwise fashion by subgraph addition. Several heuristics are being explored to restrict the combinatorial explosion that is inherent in structure generation. These include the use of generalized molecular fragments, called templates, as building blocks. Structure generation consists of two stages: (i) the generation of skeletons from templates that satisfy steric constraints and (ii) the substitution of heteroatoms into skeletons to produce molecules that satisfy other constraints such as electrostatics. The choice and definition of the templates and template joining rules are described together with a description of the atom substitution process.},
	issn = {0095-2338},
	doi = {10.1021/ci00025a016},
	author = {MATA, P and GILLET, VJ and JOHNSON, AP and Lampreia, J and MYATT, GJ and SIKE, S and STEBBINGS, AL}
}
@article { ISI:A1994NB53000038,
	title = {PRIMARY SEQUENCE, OXIDATION-REDUCTION POTENTIALS AND TERTIARY-STRUCTURE PREDICTION OF DESULFOVIBRIO-DESULFURICANS ATCC-27774 FLAVODOXIN},
	journal = {EUROPEAN JOURNAL OF BIOCHEMISTRY},
	volume = {220},
	number = {3},
	year = {1994},
	month = {MAR 15},
	pages = {987-995},
	abstract = {Flavodoxin was isolated and purified from Desulfovibrio desulfuricans ATCC 27774, a sulfatereducing organism that can also utilize nitrate as an alternative electron acceptor. Mid-point oxidation-reduction potentials of this flavodoxin were determined by ultraviolet/visible and EPR methods coupled to potentiometric measurements and their pH dependence studied in detail. The redox potential E(2), for the couple oxidized/semiquinone forms at pH 6.7 and 25 degrees C is -40 mV, while the value for the semiquinone/hydroquinone forms (E(1)), at the same pH, -387 mV. E(2) varies linearly with pH, while E(1) is independent of pH at high values. However, at low pH (<7.0), this value is less negative, compatible with a redox-linked protonation of the flavodoxin hydroquinone. A comparative study is presented for Desulfovibrio salexigens NCIB 8403 flavodoxin {[}Moura, I., Moura, J. J. G., Bruschi, M. and LeGall, J. (1980) Biochim. Biophys. Acta 591, 1-8]. The complete primary amino acid sequence was obtained by automated Edman degradation from peptides obtained by chemical and enzymic procedures. The amino acid sequence was confirmed by FAB/MS. Using the previously determined tridimensional structure of Desulfovibrio vulgaris flavodoxin as a model {[}similarity, 48,6\%; Watenpaugh, K. D., Sieker, L. C., Jensen, L. H., LeGall, J. and Dubourdieu M. (1972) Proc. Natl Acad. Sci. USA 69, 3185-3188], the tridimensional structure of D. desulfuricans ATCC 27774 flavodoxin was predicted using AMBER force-field calculations.},
	issn = {0014-2956},
	doi = {10.1111/j.1432-1033.1994.tb18703.x},
	author = {CALDEIRA, J and PALMA, PN and REGALLA, M and Lampreia, J and Calvete, J and SCHAFER, W and LeGall, J and Moura, I and Moura, JJG}
}
@inbook { ISI:A1994BB62R00016,
	title = {ADENYLYLSULFATE REDUCTASES FROM SULFATE-REDUCING BACTERIA},
	booktitle = {INORGANIC MICROBIAL SULFUR METABOLISM},
	series = {METHODS IN ENZYMOLOGY},
	volume = {243},
	year = {1994},
	pages = {241-260},
	issn = {0076-6879},
	author = {Lampreia, J and Pereira, AS and Moura, JJG}
}
@article { ISI:A1991GR96100052,
	title = {SPECTROSCOPIC STUDIES ON APS REDUCTASE ISOLATED FROM THE HYPERTHERMOPHILIC SULFATE-REDUCING ARCHAEBACTERIUM ARCHAEGLOBUS-FULGIDUS},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {181},
	number = {1},
	year = {1991},
	month = {NOV 27},
	pages = {342-347},
	issn = {0006-291X},
	doi = {10.1016/S0006-291X(05)81424-X},
	author = {Lampreia, J and Fauque, G and SPEICH, N and DAHL, C and Moura, I and TRUPER, HG and Moura, JJG}
}
@article { ISI:A1990CX62700021,
	title = {THE ACTIVE-CENTERS OF ADENYLYLSULFATE REDUCTASE FROM DESULFOVIBRIO-GIGAS - CHARACTERIZATION AND SPECTROSCOPIC STUDIES},
	journal = {EUROPEAN JOURNAL OF BIOCHEMISTRY},
	volume = {188},
	number = {3},
	year = {1990},
	month = {MAR 30},
	pages = {653-664},
	issn = {0014-2956},
	doi = {10.1111/j.1432-1033.1990.tb15447.x},
	author = {Lampreia, J and Moura, I and TEIXEIRA, M and PECK, HD and LeGall, J and HUYNH, BH and Moura, JJG}
}
@article { ISI:A1988P268600015,
	title = {IMMUNOCYTOCHEMICAL LOCALIZATION OF APS REDUCTASE AND BISULFITE REDUCTASE IN 3 DESULFOVIBRIO SPECIES},
	journal = {ARCHIVES OF MICROBIOLOGY},
	volume = {150},
	number = {3},
	year = {1988},
	month = {JUL},
	pages = {296-301},
	issn = {0302-8933},
	doi = {10.1007/BF00407795},
	author = {KREMER, DR and VEENHUIS, M and Fauque, G and PECK, HD and LeGall, J and Lampreia, J and Moura, JJG and HANSEN, TA}
}
@article { ISI:A1987J297100090,
	title = {ADENYLYL SULFATE (APS) REDUCTASE FROM DESULFOVIBRIO-GIGAS},
	journal = {RECUEIL DES TRAVAUX CHIMIQUES DES PAYS-BAS-JOURNAL OF THE ROYAL NETHERLANDS CHEMICAL SOCIETY},
	volume = {106},
	number = {6-7},
	year = {1987},
	month = {JUN-JUL},
	pages = {234},
	issn = {0165-0513},
	author = {Lampreia, J and Moura, I and Fauque, G and XAVIER, AV and LeGall, J and PECK, HD and Moura, JJG}
}
