[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B;
PubMed=2550423 [NCBI, ExPASy, EBI, Israel, Japan]
Ostrowski J.,
Barber M.J.,
Rueger D.C.,
Miller B.E.,
Siegel L.M.,
Kredich N.M.;
"Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase.";
J. Biol. Chem. 264:15796-15808(1989).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R.,
Plunkett G. III,
Bloch C.A.,
Perna N.T.,
Burland V.,
Riley M.,
Collado-Vides J.,
Glasner J.D.,
Rode C.K.,
Mayhew G.F.,
Gregor J.,
Davis N.W.,
Kirkpatrick H.A.,
Goeden M.A.,
Rose D.J.,
Mau B.,
Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K.,
Morooka N.,
Yamamoto Y.,
Fujita K.,
Isono K.,
Choi S.,
Ohtsubo E.,
Baba T.,
Wanner B.L.,
Mori H.,
Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 594-599.
STRAIN=B;
PubMed=2670946 [NCBI, ExPASy, EBI, Israel, Japan]
Ostrowski J.,
Wu J.-Y.,
Rueger D.C.,
Miller B.E.,
Siegel L.M.,
Kredich N.M.;
"Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase.";
J. Biol. Chem. 264:15726-15737(1989).
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[5]
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CHARACTERIZATION OF FAD AND FMN DOMAINS.
DOI=10.1016/0014-5793(95)01081-O; PubMed=7589518 [NCBI, ExPASy, EBI, Israel, Japan]
Eschenbrenner M.,
Coves J.,
Fontecave M.;
"NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction.";
FEBS Lett. 374:82-84(1995).
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[6]
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CHARACTERIZATION AS A NADPH:FLAVIN OXIDOREDUCTASE.
DOI=10.1074/jbc.270.35.20550; PubMed=7657631 [NCBI, ExPASy, EBI, Israel, Japan]
Eschenbrenner M.,
Coves J.,
Fontecave M.;
"The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.";
J. Biol. Chem. 270:20550-20555(1995).
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[7]
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CHARACTERIZATION OF FMN DOMAIN 1-220.
DOI=10.1021/bi9623744; PubMed=9153434 [NCBI, ExPASy, EBI, Israel, Japan]
Coves J.,
Zeghouf M.,
Macherel D.,
Guigliarelli B.,
Asso M.,
Fontecave M.;
"Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli.";
Biochemistry 36:5921-5928(1997).
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[8]
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CHARACTERIZATION AS A NADPH-CYTOCHROME P450 REDUCTASE.
DOI=10.1006/bbrc.1998.8671; PubMed=9618257 [NCBI, ExPASy, EBI, Israel, Japan]
Zeghouf M.,
Defaye G.,
Fontecave M.,
Coves J.;
"The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase.";
Biochem. Biophys. Res. Commun. 246:602-605(1998).
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[9]
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CHARACTERIZATION.
DOI=10.1021/bi9728699; PubMed=9558350 [NCBI, ExPASy, EBI, Israel, Japan]
Zeghouf M.,
Fontecave M.,
Macherel D.,
Coves J.;
"The flavoprotein component of the Escherichia coli sulfite reductase: expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors.";
Biochemistry 37:6114-6123(1998).
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[10]
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CHARACTERIZATION OF FAD DOMAIN.
DOI=10.1042/0264-6021:3420465; PubMed=10455035 [NCBI, ExPASy, EBI, Israel, Japan]
Coves J.,
Lebrun C.,
Gervasi G.,
Dalbon P.,
Fontecave M.;
"Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride.";
Biochem. J. 342:465-472(1999).
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[11]
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CHARACTERIZATION, AND STRUCTURE BY NMR OF 53-220.
DOI=10.1021/bi016008i; PubMed=11888295 [NCBI, ExPASy, EBI, Israel, Japan]
Champier L.,
Sibille N.,
Bersch B.,
Brutscher B.,
Blackledge M.,
Coves J.;
"Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain.";
Biochemistry 41:3770-3780(2002).
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[12]
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QUATERNARY STRUCTURE.
DOI=10.1074/jbc.M005619200; PubMed=10984484 [NCBI, ExPASy, EBI, Israel, Japan]
Zeghouf M.,
Fontecave M.,
Coves J.;
"A simplifed functional version of the Escherichia coli sulfite reductase.";
J. Biol. Chem. 275:37651-37656(2000).
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[13]
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X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 226-599.
DOI=10.1006/jmbi.2000.3748; PubMed=10860732 [NCBI, ExPASy, EBI, Israel, Japan]
Gruez A.,
Pignol D.,
Zeghouf M.,
Coves J.,
Fontecave M.,
Ferrer J.-L.,
Fontecilla-Camps J.-C.;
"Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module.";
J. Mol. Biol. 299:199-212(2000).
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