Nitrogenase of Klebsiella pneumoniae: electron-paramagnetic-resonance studies on the catalytic mechanism.
作者信息
Smith B E, Lowe D J, Bray R C
出版信息
Biochem J. 1972 Nov;130(2):641-3. doi: 10.1042/bj1300641.
Abstract
摘要
相似文献
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Nitrogenase of Klebsiella pneumoniae: electron-paramagnetic-resonance studies on the catalytic mechanism.肺炎克雷伯菌的固氮酶：关于催化机制的电子顺磁共振研究
Biochem J. 1972 Nov;130(2):641-3. doi: 10.1042/bj1300641.
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Electron-paramagnetic-resonance studies on nitrogenase of Klebsiella pneumoniae. Evidence for acetylene- and ethylene-nitrogenase transient complexes.肺炎克雷伯菌固氮酶的电子顺磁共振研究。乙炔和乙烯固氮酶瞬态复合物的证据。
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Nitrogenase of Klebsiella pneumoniae: interaction with viologen dyes as measured by acetylene reduction.肺炎克雷伯菌的固氮酶：通过乙炔还原法测定其与紫精染料的相互作用
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Evidence on intramolecular electron transfer in the MoFe protein of nitrogenase from Klebsiella pneumoniae from rapid-freeze electron-paramagnetic-resonance studies of its oxidation by ferricyanide.通过对肺炎克雷伯菌固氮酶的钼铁蛋白被铁氰化物氧化的快速冷冻电子顺磁共振研究，获取其分子内电子转移的证据。
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Klebsiella pneumoniae nitrogenase: pre-steady-state absorbance changes show that redox changes occur in the MoFe protein that depend on substrate and component protein ratio; a role for P-centres in reducing dinitrogen?肺炎克雷伯菌固氮酶：稳态前吸光度变化表明，钼铁蛋白中的氧化还原变化取决于底物和组分蛋白比例；P中心在还原氮气中起作用？
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Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae.肺炎克雷伯菌固氮酶催化机制的电子顺磁共振研究。
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Purification and characterization of the inactive MoFe protein (NifB-Kp1) of the nitrogenase from nifB mutants of Klebsiella pneumoniae.肺炎克雷伯氏菌nifB突变体固氮酶无活性钼铁蛋白（NifB-Kp1）的纯化与表征
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The inactive MoFe protein (NifB-Kp1) of the nitrogenase from nifB mutants of Klebsiella pneumoniae. Its interaction with FeMo-cofactor and the properties of the active MoFe protein formed.肺炎克雷伯菌nifB突变体固氮酶的无活性钼铁蛋白（NifB-Kp1）。它与铁钼辅因子的相互作用以及形成的活性钼铁蛋白的性质。
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Mössbauer spectroscopy of the nitrogenase proteins from Klebsiella pneumoniae. Structural assignments and mechanistic conclusions.肺炎克雷伯菌固氮酶蛋白的穆斯堡尔光谱。结构归属与机理结论。
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Nitrogenase of Klebsiella pneumoniae. Interaction of the component proteins studied by ultracentrifugation.肺炎克雷伯菌的固氮酶。通过超速离心研究组分蛋白的相互作用。
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本文引用的文献
1
Sudden freezing as a technique for the study of rapid reactions.骤冷法作为一种研究快速反应的技术。
Biochem J. 1961 Oct;81(1):189-93. doi: 10.1042/bj0810189.
2
EPR studies of nitrogenase: ATP dependent oxidation of fraction 1 protein by cyanide.
FEBS Lett. 1971 Jul 1;15(4):317-319. doi: 10.1016/0014-5793(71)80647-6.
3
Evidence from Mossbauer spectroscopy for the role of iron in nitrogen fixation.
Biochim Biophys Acta. 1970 Nov 3;223(1):86-104. doi: 10.1016/0005-2728(70)90134-9.
4
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.
5
Interaction of nitrogenase from Klebsiella pneumoniae with ATP or cyanide.肺炎克雷伯菌固氮酶与ATP或氰化物的相互作用。
Biochim Biophys Acta. 1970;205(2):288-99. doi: 10.1016/0005-2728(70)90258-6.
6
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.
7
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.
8
Kinetic studies on Klebsiella pneumoniae nitrogenase.肺炎克雷伯氏菌固氮酶的动力学研究。
Proc Natl Acad Sci U S A. 1971 Sep;68(9):2016-8. doi: 10.1073/pnas.68.9.2016.
9
A reevaluation of the presence of low midpoint potential cytochrome 551.5 in the green photosynthetic bacterium Chloropseudomonas ethylica.对绿色光合细菌嗜乙基绿假单胞菌中低中点电位细胞色素551.5存在情况的重新评估。
Biochem Biophys Res Commun. 1972 Apr 28;47(2):322-7. doi: 10.1016/0006-291x(72)90715-2.
10
Spin-spin interaction between molybdenum and one of the iron-sulphur systems of xanthine oxidase and its relevance to the enzymic mechanism.钼与黄嘌呤氧化酶的铁硫系统之一之间的自旋-自旋相互作用及其与酶促机制的相关性。
Biochem J. 1972 Nov;130(1):239-49. doi: 10.1042/bj1300239.
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