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A free radical flavoprotein from Azotobacter. Isolation, crystallization, and properties.

作者信息

Hinkson J W, Bulen W A

出版信息

J Biol Chem. 1967 Jul 25;242(14):3345-51.

PMID:6029442
Abstract
摘要

相似文献

1
A free radical flavoprotein from Azotobacter. Isolation, crystallization, and properties.一种来自固氮菌的自由基黄素蛋白。分离、结晶及性质
J Biol Chem. 1967 Jul 25;242(14):3345-51.
2
Azotobacter free-radical flavoprotein. Preparation and properties of the apoprotein.固氮菌自由基黄素蛋白。脱辅基蛋白的制备及性质
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3
Flavine-protein interactions in flavoenzymes. Effect of chemical modification of tryptophan residues upon flavine mononucleotide binding and protein fluorescence in Azotobacter flavodoxin.
Biochemistry. 1973 Oct 23;12(22):4550-4. doi: 10.1021/bi00746a039.
4
Flavodoxin from Azotobacter vinelandii.
Arch Mikrobiol. 1972;82(2):155-72. doi: 10.1007/BF01890407.
5
Chemical and physical characterization of the Shethna flavoprotein and apoprotein and kinetics and thermodynamics of flavin analog binding to the apoprotein.谢特那黄素蛋白和脱辅基蛋白的化学与物理特性以及黄素类似物与脱辅基蛋白结合的动力学和热力学
Biochemistry. 1971 Jan 5;10(1):124-32. doi: 10.1021/bi00777a019.
6
Oxidation--reduction properties of phytoflavin, a flavoprotein from blue-green algae.
Arch Biochem Biophys. 1972 Aug;151(2):378-86. doi: 10.1016/0003-9861(72)90512-7.
7
Purification and some properties of molybdoferredoxin, a component of nitrogenase from Clostridium pasteurianum.巴氏芽孢梭菌固氮酶组分钼铁氧还蛋白的纯化及其某些性质
Biochemistry. 1971 May 25;10(11):2066-72. doi: 10.1021/bi00787a016.
8
Two biologically active ferredoxins from the aerobic nitrogen-fixing bacteriu, Azotobacter vinelandii.来自需氧固氮细菌维涅兰德固氮菌的两种具有生物活性的铁氧化还原蛋白。
J Biol Chem. 1972 Jul 25;247(14):4514-20.
9
A 13C nuclear-magnetic-resonance study on free flavins and Megasphaera elsdenii and Azotobacter vinelandii flavodoxin. 13C-enriched flavins as probes for the study of flavoprotein active sites.
Eur J Biochem. 1981 Nov;120(1):33-9. doi: 10.1111/j.1432-1033.1981.tb05666.x.
10
Purification and properties of two iron-sulfur proteins from Azotobacter vinelandii.来自棕色固氮菌的两种铁硫蛋白的纯化及性质
Biochim Biophys Acta. 1969 Dec 23;194(2):548-63. doi: 10.1016/0005-2795(69)90117-2.

引用本文的文献

1
Flavodoxin hydroquinone reduces Azotobacter vinelandii Fe protein to the all-ferrous redox state with a S = 0 spin state.黄素氧还蛋白对苯二酚将棕色固氮菌铁蛋白还原为具有S = 0自旋态的全亚铁氧化还原状态。
Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17131-6. doi: 10.1073/pnas.0603223103. Epub 2006 Nov 3.
2
The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.棕色固氮菌脱辅基黄素氧还蛋白II的平衡去折叠过程通过一个相对稳定的折叠中间体发生。
Protein Sci. 1998 Nov;7(11):2331-44. doi: 10.1002/pro.5560071110.
3
Structure-function relations in flavodoxins.
黄素氧还蛋白中的结构-功能关系
Mol Cell Biochem. 1980 Dec 10;33(1-2):13-24. doi: 10.1007/BF00224568.
4
Purification and some properties of a non-haem iron protein from the bacteroids of soya-bean (Glycine max Merr) nodules.来自大豆（Glycine max Merr）根瘤类菌体的一种非血红素铁蛋白的纯化及某些性质
Biochem J. 1970 Aug;118(5):773-81. doi: 10.1042/bj1180773.
5
The electron transport system in nitrogen fixation by Azotobacter. I. Azotoflavin as an electron carrier.固氮菌固氮过程中的电子传递系统。I. 偶氮黄素作为电子载体。
Proc Natl Acad Sci U S A. 1969 Nov;64(3):1079-86. doi: 10.1073/pnas.64.3.1079.
6
Nature of oxygen inhibition of nitrogenase from Azotobacter vinelandii.维涅兰德固氮菌中固氮酶的氧抑制特性
Proc Natl Acad Sci U S A. 1972 Mar;69(3):672-5. doi: 10.1073/pnas.69.3.672.
7
Flavodoxin from Azotobacter vinelandii.
Arch Mikrobiol. 1972;82(2):155-72. doi: 10.1007/BF01890407.
8
The electron transport system in nitrogen fixation by Azotobacter. II. Isolation and function of a new type of ferredoxin.固氮菌固氮过程中的电子传递系统。II. 一种新型铁氧化还原蛋白的分离与功能
Proc Natl Acad Sci U S A. 1969 Dec;64(4):1404-10. doi: 10.1073/pnas.64.4.1404.
9
Covalently bound non-coenzyme phosphorus residues in flavoproteins: 31P nuclear magnetic resonance studies of Azotobacter flavodoxin.黄素蛋白中与共价结合的非辅酶磷残基：固氮菌黄素氧还蛋白的31P核磁共振研究
Proc Natl Acad Sci U S A. 1979 Aug;76(8):3786-9. doi: 10.1073/pnas.76.8.3786.
10
Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle.固氮酶和固氮酶还原酶在每个催化循环中结合和解离。
Proc Natl Acad Sci U S A. 1978 Jun;75(6):2699-702. doi: 10.1073/pnas.75.6.2699.