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Общее количество найденных документов : 53
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1.
| Young Lawrence J. Superoxidized states of Escherichia coli sulfite reductase heme protein subunit // Biochemistry, 1988. Vol. 27, N 16.-С.5984-5990
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2.
| Hallenbeck Patrick C. Characterization of anaerobic sulfite reduction by Salmonella typhimurium and purification of the anaerobically induced sulfite reductase // J. Bacteriol., 1989. Vol. 171, N 6.-С.3008-3015
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3.
| Изерская Л.А. Формы серы и активность ферментов серного обмена в полугидроморфных почвах // Тез. докл. 8 Всес. съезда почвоведов, Новосибирск, 14-18 авт., 1989. -Новосибирск, 1989, Кн. 3 Комис. 4.-С.11
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4.
| Ostrowski Molecular characterization of the cysJIH promoters of Salmonella typhimurium and Escherichia coli: regulation by cysB protein and N-acetyl-Lserine // J. Bacteriol., 1989. Vol. 171, N 1.-С.130-140
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5.
| Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemicabl and catalytic protperties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with nadph-cytochrome P-450 reductase // J. Biol. Chem., 1989. Vol. 264, N 27.-С.15796-15808
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6.
| Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B // J. Biol. Chem., 1989. Vol. 264, N 26.-С.15726-15737
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7.
| Young Lawrence J. Alkaline low spin form of sulfite reductase hemeprotein subunit // Biochem. and Biophys. Res. Commun., 1990. Vol. 169, N 1.-С.39-45
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| Siegel Lewis M. Structure and function of the bridged siroheme - Fe[4]S[4] active center of assimilatory sulfite and nitrite reductases // Bio Factors, 1991. Vol. 3, N 2.-С.141-142
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9.
| Direct evidence of the metal-free nature of sirohydrochlorin in desulfoviridin // Biochim. et Biophys. acta. Bioenerg., 1991. Vol. 1060, N 1.-С.25-27
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10.
| Wu High-level expression of Escherichia coli NADPH-sulfite reductase: Requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor // J. Bacteriol., 1991. Vol. 173, N 1.-С.325-333
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11.
| Physicochemical and spectroscopic properties of adenylyl sulfate reductase from the marine hyperthermophilic sulfate reducing archaebacterium Archaeoglobus fulgidus // Int. Conf. Thermophiles: Sci. and Technol., Reykjavik, 23rd - 26th Aug., 1992. -Reykjavik, 1992.-С.141
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12.
| Physicochemical and spectroscopic properties of adenylyl sulfate reductase from the marine hyperthermophilic sulfate-reducing archaebacterium Archaeoglobus fulgidus // Int. Conf. Thermophiles. -Reykjavik, 1992.-С.141
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13.
| Wolfe Bonnie M. Desulfoviridin, a multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough): Purification, characterization, kinetics and EPR studies // Eur. J. Biochem., 1994. Vol. 223, N 1.-С.79-89
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14.
| Eschenbrenner 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. Vol. 270, N 35.-С.20550-20555
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15.
| Eschenbrenner NADPH-sulfite reductase flavoprotein from Escherichia coli: Contribution to the flavin content and subunit interaction // FEBS Lett., 1995. Vol. 374, N 1.-С.82-84
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16.
| Belinsky Moisey I. Exchange model of the {[Fe[4]S[4]]-Fe} active site of sulfite reductase // Chem. Phys., 1995. Vol. 201, N 2-3.-С.343-356
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17.
| Belinsky Moisey I. Induced paramagnetism and hyperfine interactions in the {[Fe[4]S[4]]-Fe} active site of Escherichia coli sulfite reductase // Chem. Phys. Lett., 1996. Vol. 250, N 3-4.-С.320-327
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18.
| Nitrite reductase from Desulfovibrio desulfuricans (ATCC 27774) - A heterooligomer heme protein with sulfite reductase activity // Biochem. and Biophys. Res. Commun., 1996. Vol. 224, N 3.-С.611-618
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19.
| Nitrite reductase from Desulfovibrio desulfuricans (ATCC 27774) - A heterooligomer heme protein with sulfite reductase activity // Biochem. and Biophys. Res. Commun., 1996. Vol. 224, N 3.-С.611-618
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20.
| Belinsky Moisey I. Induced paramagnetism and hyperfine interactions in the {[Fe[4]S[4]]-Fe} active site of Escherichia coli sulfite reductase // Chem. Phys. Lett., 1996. Vol. 250, N 3-4.-С.320-327
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