cysI

Summary

Gene Symbol: cysI
Description: sulfite reductase, beta subunit, NAD(P)-binding, heme-binding
Alias: ECK2758, JW2733
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Gaudu P, Fontecave M. The NADPH: sulfite reductase of Escherichia coli is a paraquat reductase. Eur J Biochem. 1994;226:459-63 pubmed
    ..These results suggest that the sulfite reductase is a major paraquat reductase in E. coli and is responsible for the toxic activation of the drug. ..
  2. Tei H, Murata K, Kimura A. Molecular cloning of the cys genes (cysC, cysD, cysH, cysI, cysJ, and cysG) responsible for cysteine biosynthesis in Escherichia coli K-12. Biotechnol Appl Biochem. 1990;12:212-6 pubmed
    ..The following results were obtained. First, the cysCDHIJ regulon could be separated into cysCD and cysHIJ regions. Second, the cysG gene was quite different from the cysI and cysJ genes.
  3. Kaufman J, Siegel L, Spicer L. Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands. Biochemistry. 1993;32:8782-91 pubmed
    ..Data are also presented for the existence of a secondary anion binding site, the occupancy of which perturbs the oxidized SiR-HP NMR spectrum, where binding occurs at a rate much faster than that of ligand binding to heme. ..
  4. Bairoch A, Boeckmann B. The SWISS-PROT protein sequence data bank, recent developments. Nucleic Acids Res. 1993;21:3093-6 pubmed
  5. Siegel L, Davis P, Kamin H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow. J Biol Chem. 1974;249:1572-86 pubmed
  6. Siegel L, Davis P. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components. J Biol Chem. 1974;249:1587-98 pubmed
  7. Faeder E, Davis P, Siegel L. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. V. Studies with the Escherichia coli hemoflavoprotein depleted of flavin mononucleotide: distinct roles for the flavin adenine dinucleotide and flavin mononucleo. J Biol Chem. 1974;249:1599-609 pubmed
  8. Murphy M, Siegel L, Kamin H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme. J Biol Chem. 1974;249:1610-4 pubmed
  9. Crane B, Siegel L, Getzoff E. Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. Science. 1995;270:59-67 pubmed
    ..An extensive hydrogen-bonding network of positive side chains, water molecules, and siroheme carboxylates activates S-O bonds for reductive cleavage. ..

More Information

Publications33

  1. Miller E, Jarboe L, Turner P, Pharkya P, Yomano L, York S, et al. Furfural inhibits growth by limiting sulfur assimilation in ethanologenic Escherichia coli strain LY180. Appl Environ Microbiol. 2009;75:6132-41 pubmed publisher
  2. Lazzarini R, Atkinson D. A triphosphopyridine nucleotide-specific nitrite reductase from Escherichia coli. J Biol Chem. 1961;236:3330-5 pubmed
  3. 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. 1998;37:6114-23 pubmed
    ..Despite the conservation of the bi-flavin-domain structure between these proteins over evolutionary time, each of them provides significantly different flavin reactivities. ..
  4. 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. 1997;36:5921-8 pubmed
    ..Moreover, the FMN prosthetic group in SiR-FP23 and native SiR-FP is compared to that of cytochrome P450 reductase and bacterial cytochrome P450, which also contain one FAD and one FMN per polypeptide chain. ..
  5. 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. 1995;270:20550-5 pubmed
    ..This result, together with the sequence homology between SiR-FP and NADPH-cytochrome P-450 reductase, suggests a new model for the structure of the protein with one FMN and one FAD prosthetic group per alpha subunit. ..
  6. Siegel L, Rueger D, Barber M, Krueger R, Orme Johnson N, Orme Johnson W. Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes. J Biol Chem. 1982;257:6343-50 pubmed
    ..The potential of the Fe4S4 center is approximately 70 mV more negative in the CN- as opposed to the CO-ligated HP (-420 mV), a result which indicates the presence of heme-Fe4S4-ligand interaction in the HP complexes. ..
  7. Christner J, Munck E, Janick P, Siegel L. Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups. J Biol Chem. 1981;256:2098-101 pubmed
    ..Thus, sulfite reductase provides the first example of an active site where a heme and an iron-sulfur cluster are closely linked as a functional unit, probably via a common bridging ligand. ..
  8. Siegel L, Murphy M, Kamin H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups. J Biol Chem. 1973;248:251-64 pubmed
  9. Hunt C, Colless V, Smith M, Molasky D, Malo M, Loughlin R. Lambda transducing phage and clones carrying genes of the cysJIHDC gene cluster of Escherichia coli K12. J Gen Microbiol. 1987;133:2707-17 pubmed
    ..The direction of transcription of the cysD gene was established, and from physical evidence the size of the 'silent section' between the cysH and cysD genes was estimated to be at least 11 kb. ..
  10. Christner J, Munck E, Janick P, Siegel L. Mössbauer evidence for exchange-coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase. Studies of the reduced states and of a nitrite turnover complex. J Biol Chem. 1983;258:11147-56 pubmed
    ..The data obtained for the reduced forms of uncomplexed enzyme show that the siroheme iron is Fe(II), that it is paramagnetic, and possibly in the S = 1 intermediate spin state. ..
  11. Krone F, Westphal G, Schwenn J. Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli. Mol Gen Genet. 1991;225:314-9 pubmed
    ..Reduction of the enzyme by dithiols resulted in a shift of the apparent molecular weight from 44,000 to 62,000 without formation of an enzyme-thioredoxin complex. ..
  12. Kemp J, Atkinson D, Ehret A, Lazzarini R. EVIDENCE FOR THE IDENTITY OF THE NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE-SPECIFIC SULFITE AND NITRITE REDUCTASES OF ESCHERICHIA COLI. J Biol Chem. 1963;238:3466-71 pubmed
  13. Crane B, Siegel L, Getzoff E. Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange. Biochemistry. 1997;36:12101-19 pubmed
    ..Reduction-gated release of phosphate from the substrate-binding site may explain the 10(5)-fold increase in rates of ligand association that accompany reduction of SiRHP. ..
  14. Li C, Peck H, Przybyla A. Cloning of the 3'-phosphoadenylyl sulfate reductase and sulfite reductase genes from Escherichia coli K-12. Gene. 1987;53:227-34 pubmed
    ..8.1.2)(cysI and cysJ) of Escherichia coli K-12 have been cloned by complementation. pCYSI contains two PstI fragments (18...
  15. Coves J, Eschenbrenner M, Fontecave M. Sulfite reductase of Escherichia coli is a ferrisiderophore reductase. Biochem Biophys Res Commun. 1993;192:1403-8 pubmed
    ..Free flavins, riboflavin, FMN, FAD were absolutely required, suggesting that this activity resides in the flavin reductase activity of sulfite reductase. ..
  16. Coves J, Niviere V, Eschenbrenner M, Fontecave M. NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase. J Biol Chem. 1993;268:18604-9 pubmed
    ..Pure sulfite reductase has the ability to catalyze the reduction of free riboflavin, FMN, or FAD by NADPH and thus, as Fre, to transfer electrons to the iron center of metR2, a key step during the activation reaction. ..
  17. Eschenbrenner M, Coves J, Fontecave M. NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction. FEBS Lett. 1995;374:82-4 pubmed
    ..One can conclude that each alpha-chain of SiR-FP is composed of two distinct domains, one binding FAD and the other FMN and that the FMN-binding domains cooperate for a head-to-head subunit interaction. ..
  18. Kaufman J, Spicer L, Siegel L. Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit. Biochemistry. 1993;32:2853-67 pubmed
    ..abstract truncated at 400 words) ..
  19. Fieschi F, Niviere V, Frier C, Decout J, Fontecave M. The mechanism and substrate specificity of the NADPH:flavin oxidoreductase from Escherichia coli. J Biol Chem. 1995;270:30392-400 pubmed
    ..coli growing cells. As a consequence, it can enhance the antiproliferative effect of hydroxyurea, a cell-specific ribonucleotide reductase inactivator. ..
  20. Crane B, Siegel L, Getzoff E. Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products. Biochemistry. 1997;36:12120-37 pubmed
    ..From the structures reported here, we propose a series of key structural states of ligated SiRHP in the catalytic reduction of sulfite to sulfide. ..
  21. Ostrowski J, Wu J, Rueger D, Miller B, Siegel L, Kredich N. 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 nitrit. J Biol Chem. 1989;264:15726-37 pubmed
    ..The DNA sequences of cysI and cysH from S. typhimurium and E...
  22. Murphy M, Siegel L, Kamin H, Rosenthal D. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. II. Identification of a new class of heme prosthetic group: an iron-tetrahydroporphyrin (isobacteriochlorin type) with eight carboxylic acid groups. J Biol Chem. 1973;248:2801-14 pubmed
  23. McRee D, Richardson D, Richardson J, Siegel L. The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase. J Biol Chem. 1986;261:10277-81 pubmed
    ..Some possible implications of the proposed structure on the role of the bridged siroheme-Fe4S4 cluster in catalysis are discussed. ..
  24. Wu J, Siegel L, Kredich N. High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor. J Bacteriol. 1991;173:325-33 pubmed
    The flavoprotein and hemoprotein components of Escherichia coli B NADPH-sulfite reductase are encoded by cysJ and cysI, respectively...