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Physical and chemical properties of the nitrogenase proteins form Azotobacter vinelandii.

作者信息

Kleiner D, Chen C H

出版信息

Arch Mikrobiol. 1974 Jun 7;98(1):93-100. doi: 10.1007/BF00425272.

DOI:10.1007/BF00425272
PMID:4834634
Abstract
摘要

相似文献

1
Physical and chemical properties of the nitrogenase proteins form Azotobacter vinelandii.棕色固氮菌固氮酶蛋白的物理和化学性质
Arch Mikrobiol. 1974 Jun 7;98(1):93-100. doi: 10.1007/BF00425272.
2
Resolution of two subunits from the molybdenum-iron protein of Azotobacter vinelandii nitrogenase.从棕色固氮菌固氮酶的钼铁蛋白中解析出两个亚基。
J Biol Chem. 1981 Dec 10;256(23):11981-3.
3
Electron microscopy of the Mo-Fe protein from Azotobacter nitrogenase.固氮菌固氮酶钼铁蛋白的电子显微镜观察
J Cell Biol. 1974 Jan;60(1):311-6. doi: 10.1083/jcb.60.1.311.
4
The molecular weight of, and evidence for two types of subunits in, the molybdenum-iron protein of Azotobacter vinelandii nitrogenase.棕色固氮菌固氮酶钼铁蛋白的分子量及两种亚基的证据
Biochem J. 1977 Jun 1;163(3):427-32. doi: 10.1042/bj1630427.
5
Some properties of the nitrogenase proteins from Clostridium pasteurianum. Molecular weight, subunit structure, isoelectric point and EPR spectra.巴氏芽孢梭菌固氮酶蛋白的一些特性。分子量、亚基结构、等电点和电子顺磁共振光谱。
Arch Microbiol. 1974;99(1):71-80. doi: 10.1007/BF00696223.
6
Nitrogenase from Azotobacter chroococcum. Purification and properties of the component proteins.来自褐球固氮菌的固氮酶。组分蛋白的纯化及特性
Eur J Biochem. 1975 Dec 15;60(2):467-76. doi: 10.1111/j.1432-1033.1975.tb21025.x.
7
Molybdenum-independent nitrogenases of Azotobacter vinelandii: a functional species of alternative nitrogenase-3 isolated from a molybdenum-tolerant strain contains an iron-molybdenum cofactor.维涅兰德固氮菌的非钼铁氮酶：从耐钼菌株中分离出的替代固氮酶-3的一种功能型含有铁钼辅因子。
Biochem J. 1993 Jul 1;293 ( Pt 1)(Pt 1):101-7. doi: 10.1042/bj2930101.
8
Nitrogenase. II. Changes in the EPR signal of component I (iron-molybdenum protein) of Azotobacter vinelandii nitrogenase during repression and derepression.固氮酶。II. 棕色固氮菌固氮酶组分I（铁钼蛋白）在阻遏和去阻遏过程中电子顺磁共振信号的变化。
Biochim Biophys Acta. 1972 Feb 28;256(2):512-23. doi: 10.1016/0005-2728(72)90079-5.
9
Nitrogenase. I. Repression and derepression of the iron-molybdenum and iron proteins of nitrogenase in Azotobacter vinelandii.固氮酶。I. 棕色固氮菌中固氮酶的铁钼蛋白和铁蛋白的阻遏与去阻遏
Biochim Biophys Acta. 1972 Feb 28;256(2):498-511. doi: 10.1016/0005-2728(72)90078-3.
10
Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Some aspects of its structure.来自棕色固氮菌的吡啶核苷酸转氢酶。其结构的某些方面。
J Biol Chem. 1972 Nov 10;247(21):6802-9.

引用本文的文献

1
High recovery of nitrogenase activity and of Fe-labeled nitrogenase in heterocysts isolated from Anabaena variabilis.从多变鱼腥藻中分离出的异形胞中，固氮酶活性和铁标记固氮酶的回收率很高。
Proc Natl Acad Sci U S A. 1978 Dec;75(12):6271-5. doi: 10.1073/pnas.75.12.6271.
2
Comparison of the iron proteins from the nitrogen fixation complexes of Azotobacter vinelandii, Clostridium pasteurianum, and Klebsiella pneumoniae.棕色固氮菌、巴氏梭菌和肺炎克雷伯氏菌固氮复合物中铁蛋白的比较。
Proc Natl Acad Sci U S A. 1980 Jul;77(7):3826-30. doi: 10.1073/pnas.77.7.3826.
3
Some properties of the nitrogenase proteins from Clostridium pasteurianum. Molecular weight, subunit structure, isoelectric point and EPR spectra.

本文引用的文献

1
STUDIES ON THE CHEMICAL NATURE OF CLOSTRIDIAL FERREDOXIN.梭菌铁氧化还原蛋白化学性质的研究。
J Biol Chem. 1963 Dec;238:3899-913.
2
A new, rapid method of determining tryptophan.一种测定色氨酸的新的快速方法。
Anal Biochem. 1963 Jul;6:69-76. doi: 10.1016/0003-2697(63)90009-5.
3
A method for determining the sedimentation behavior of enzymes: application to protein mixtures.一种测定酶沉降行为的方法：应用于蛋白质混合物
巴氏芽孢梭菌固氮酶蛋白的一些特性。分子量、亚基结构、等电点和电子顺磁共振光谱。
Arch Microbiol. 1974;99(1):71-80. doi: 10.1007/BF00696223.
4
Interactions of heterologous nitrogenase components that generate catalytically inactive complexes.产生无催化活性复合物的异源固氮酶组分间的相互作用。
Proc Natl Acad Sci U S A. 1976 Dec;73(12):4369-73. doi: 10.1073/pnas.73.12.4369.
5
Selective inactivation of nitrogenase in Azotobacter vinelandii batch cultures.在棕色固氮菌分批培养物中对固氮酶进行选择性失活。
J Bacteriol. 1976 Oct;128(1):117-22. doi: 10.1128/jb.128.1.117-122.1976.
6
The molecular weight of, and evidence for two types of subunits in, the molybdenum-iron protein of Azotobacter vinelandii nitrogenase.棕色固氮菌固氮酶钼铁蛋白的分子量及两种亚基的证据
Biochem J. 1977 Jun 1;163(3):427-32. doi: 10.1042/bj1630427.
7
The molybdenum--iron protein of Klebsiella pneumoniae nitrogenase. Evidence for non-identical subunits from peptide 'mapping'.肺炎克雷伯氏菌固氮酶的钼铁蛋白。来自肽“图谱分析”的不同亚基的证据。
Biochem J. 1976 May 1;155(2):383-9. doi: 10.1042/bj1550383.
8
Isolation of an iron-molybdenum cofactor from nitrogenase.从固氮酶中分离出铁钼辅因子。
Proc Natl Acad Sci U S A. 1977 Aug;74(8):3249-53. doi: 10.1073/pnas.74.8.3249.
9
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.
10
Possible evolutionary relationships of the nitrogenase proteins.固氮酶蛋白可能的进化关系。
J Mol Evol. 1976 Mar 29;7(2):159-65. doi: 10.1007/BF01732473.
J Biol Chem. 1961 May;236:1372-9.
4
A micro biuret method for protein determination; determination of total protein in cerebrospinal fluid.一种用于蛋白质测定的微量双缩脲法；脑脊液中总蛋白的测定
Scand J Clin Lab Invest. 1953;5(3):218-22. doi: 10.3109/00365515309094189.
5
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定分子量的可靠性。
J Biol Chem. 1969 Aug 25;244(16):4406-12.
6
Formation of the nitrogen-fixing enzyme system in Azotobacter vinelandii.棕色固氮菌中固氮酶系统的形成。
Can J Microbiol. 1968 Jan;14(1):25-31. doi: 10.1139/m68-005.
7
Molecular weight and subunit structure of molybdoferredoxin from Clostridium pasteurianum W5.
Biochim Biophys Acta. 1971 Feb 16;229(2):431-6. doi: 10.1016/0005-2795(71)90202-9.
8
Isolation by crystallization of the Mo-Fe protein of Azotobacter nitrogenase.通过结晶法分离固氮菌固氮酶的钼铁蛋白。
Biochem Biophys Res Commun. 1970 Apr 8;39(1):90-9. doi: 10.1016/0006-291x(70)90762-x.
9
Mechanism of the enzymic reduction of N2: the binding of adenosine 5'-triphosphate and cyanide to the N2-reducing system.N2酶促还原的机制：腺苷5'-三磷酸和氰化物与N2还原系统的结合。
Proc Natl Acad Sci U S A. 1968 Nov;61(3):1021-7. doi: 10.1073/pnas.61.3.1021.
10
The nitrogenase system from Azotobacter: two-enzyme requirement for N2 reduction, ATP-dependent H2 evolution, and ATP hydrolysis.来自固氮菌的固氮酶系统：N₂还原需要两种酶、ATP依赖性H₂生成以及ATP水解。
Proc Natl Acad Sci U S A. 1966 Sep;56(3):979-86. doi: 10.1073/pnas.56.3.979.