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肺炎克雷伯菌的固氮酶。三磷酸镁诱导的组分蛋白间电子转移的停流研究。

Nitrogenase of Klebsiella pneumoniae. A stopped-flow study of magnesium-adenosine triphosphate-induce electron transfer between the compeonent proteins.

作者信息

Thorneley R N

出版信息

Biochem J. 1975 Feb;145(2):391-6. doi: 10.1042/bj1450391.

DOI:10.1042/bj1450391
PMID:1098654
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1165229/
Abstract

Stopped-flow kinetic data have been obtained for a rapid electron-transfer reaction between the component proteins of nitrogenase from Klebsiella pneumoniae, which was induced by MgATP. Up to three equivalents of the Fe-containing protein were rapidly oxidized by one equivalent of the Fe-Mo-containing protein in a unimolecular reaction, k2 = 2 x 10(2)S-1. Evidence for a tight complex between the component proteins, KD(complex) less than 0.5 muM, which was formed with a rate k1 greater than 1 x 10(7)M-1-S-1, has been obtained. MgATP bound to either the Fe-containing protein or to the two-protein complex with a rate k3 greater than 2.5 x 10(6)M-1-S-1 and with KD(MgATP) = 0.4mM, before the electron-transfer reaction.

摘要

已获得肺炎克雷伯菌固氮酶各组成蛋白之间由MgATP诱导的快速电子转移反应的停流动力学数据。在单分子反应中，一当量含Fe-Mo的蛋白能快速氧化多达三当量的含铁蛋白，二级反应速率常数k2 = 2×10² s⁻¹。已获得证据表明各组成蛋白之间形成了紧密复合物，解离常数KD(复合物)小于0.5 μM，其形成速率k1大于1×10⁷ M⁻¹·s⁻¹。在电子转移反应之前，MgATP以速率k3大于2.5×10⁶ M⁻¹·s⁻¹且解离常数KD(MgATP)=0.4 mM的方式与含铁蛋白或双蛋白复合物结合。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8db8/1165229/36bf2f9bb213/biochemj00566-0266-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8db8/1165229/36bf2f9bb213/biochemj00566-0266-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8db8/1165229/36bf2f9bb213/biochemj00566-0266-a.jpg

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MgATP-independent hydrogen evolution catalysed by nitrogenase: an explanation for the missing electron(s) in the MgADP-AlF4 transition-state complex.固氮酶催化的不依赖MgATP的析氢反应：对MgADP-AlF4过渡态复合物中缺失电子的解释
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