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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 mononucleotide prosthetic groups in catalysis.

作者信息

Faeder E J, Davis P S, Siegel L M

出版信息

J Biol Chem. 1974 Mar 10;249(5):1599-609.

PMID:4150392
Abstract
摘要

相似文献

1
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 mononucleotide prosthetic groups in catalysis.肠道细菌的还原型烟酰胺腺嘌呤二核苷酸磷酸 - 亚硫酸盐还原酶。V. 对缺乏黄素单核苷酸的大肠杆菌血红素黄素蛋白的研究：黄素腺嘌呤二核苷酸和黄素单核苷酸辅基在催化中的不同作用。
J Biol Chem. 1974 Mar 10;249(5):1599-609.
2
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow.肠道细菌的还原型烟酰胺腺嘌呤二核苷酸磷酸 - 亚硫酸盐还原酶。3. 大肠杆菌血红素黄素蛋白：催化参数及电子传递顺序。
J Biol Chem. 1974 Mar 10;249(5):1572-86.
3
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups.肠道细菌的还原型烟酰胺腺嘌呤二核苷酸磷酸 - 亚硫酸盐还原酶。I. 大肠杆菌血红素黄素蛋白：分子参数和辅基
J Biol Chem. 1973 Jan 10;248(1):251-64.
4
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 Mar 10;249(5):1587-98.
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Flavin interaction in NADPH-sulfite reductase.黄素在NADPH-亚硫酸盐还原酶中的相互作用。
Z Naturforsch B Anorg Chem Org Chem Biochem Biophys Biol. 1972 Sep;27(9):1087-9. doi: 10.1515/znb-1972-0929.
6
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 Mar 10;249(5):1610-4.
7
The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.来自大肠杆菌的亚硫酸盐还原酶黄素蛋白组分的黄素还原酶活性。一种蛋白质结构的新模型。
J Biol Chem. 1995 Sep 1;270(35):20550-5. doi: 10.1074/jbc.270.35.20550.
8
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.大肠杆菌亚硫酸盐还原酶的黄素蛋白组分：含有黄素腺嘌呤二核苷酸和黄素单核苷酸辅因子的单体形式的表达、纯化及其光谱和催化特性
Biochemistry. 1998 Apr 28;37(17):6114-23. doi: 10.1021/bi9728699.
9
Studies on yeast sulfite reductase. I. Purification and characterization.酵母亚硫酸盐还原酶的研究。I. 纯化与特性鉴定。
Biochim Biophys Acta. 1968 Apr 2;153(3):555-75. doi: 10.1016/0005-2728(68)90185-0.
10
Studies on yeast sulfite reductase. II. Partial purification and properties of genetically incomplete sulfite reductases.酵母亚硫酸盐还原酶的研究。II. 基因不完全的亚硫酸盐还原酶的部分纯化及性质
Biochim Biophys Acta. 1968 Apr 2;153(3):576-88. doi: 10.1016/0005-2728(68)90186-2.

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Structural and biochemical elucidation of class I hybrid cluster protein natively extracted from a marine methanogenic archaeon.从海洋产甲烷古菌中天然提取的I类杂交簇蛋白的结构与生化解析
Front Microbiol. 2023 May 11;14:1179204. doi: 10.3389/fmicb.2023.1179204. eCollection 2023.
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A salvage pathway maintains highly functional respiratory complex I.一种补救途径维持着高度功能性的呼吸复合物 I。
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3
The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly.
大肠杆菌同化型NADPH-亚硫酸盐还原酶血红蛋白的N端结构域是介导全酶组装的寡聚化结构域。
J Biol Chem. 2015 Jul 31;290(31):19319-33. doi: 10.1074/jbc.M115.662379. Epub 2015 Jun 18.
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Characterization of anaerobic sulfite reduction by Salmonella typhimurium and purification of the anaerobically induced sulfite reductase.鼠伤寒沙门氏菌厌氧亚硫酸盐还原特性及厌氧诱导亚硫酸盐还原酶的纯化
J Bacteriol. 1989 Jun;171(6):3008-15. doi: 10.1128/jb.171.6.3008-3015.1989.
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Bacterial iron-sulfur proteins.细菌铁硫蛋白
Microbiol Rev. 1979 Sep;43(3):384-421. doi: 10.1128/mr.43.3.384-421.1979.