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肺炎克雷伯菌的固氮酶。关于二价金属离子和核苷酸与铁蛋白结合的水质子核磁共振弛豫研究。

Nitrogenase of Klebsiella pneumoniae. Water proton NMR relaxation studies on the binding of divalent metal ions and nucleotides to the iron protein.

作者信息

Bishop E O, Lambert M D, Orchard D, Smith B E

出版信息

Biochim Biophys Acta. 1977 Jun 10;482(2):286-300. doi: 10.1016/0005-2744(77)90242-x.

DOI:10.1016/0005-2744(77)90242-x
PMID:328053
Abstract

Interactions between the iron protein, Kp2, of nitrogenase manganese ions, magnesium ions, and the nucleotides ATP or ADP, have been studied in aqueous solution by monitoring the water proton NMR relaxation rate enhancement caused by Mn2+. Binding of Mn2+ to a molecule of Kp2 occurs at four sites, indistinguishable within experimental error, having a Kd = 350 +/- 50 micron. The Mn2+ - Kp2 complex has a low characteristic enhancement (epsilonb = 6 +/- 0.5). All four sites can alternatively bind Mg2+, not necessarily with the same dissociation constant, but with a mean Kd = 1.7 +/- 0.3 mM. Ternary complexes with the configuration EMS or (formula: see text) are formed between Kp2, Mn2+ and nucleotide (ATP or ADP). The ternary complexes with Mg2+ in place of Mn2+ probably have the latter configuration. A novel treatment of enhancement data (a 'high metal' approximation) is given.

摘要

通过监测由Mn2+引起的水质子NMR弛豫速率增强，已在水溶液中研究了固氮酶的铁蛋白Kp2、锰离子、镁离子与核苷酸ATP或ADP之间的相互作用。Mn2+与一个Kp2分子在四个位点结合，在实验误差范围内无法区分，解离常数Kd = 350 +/- 50微摩尔。Mn2+ - Kp2复合物具有较低的特征增强值（εb = 6 +/- 0.5）。所有四个位点都可以选择性地结合Mg2+，解离常数不一定相同，但平均Kd = 1.7 +/- 0.3毫摩尔。在Kp2、Mn2+和核苷酸（ATP或ADP）之间形成了构型为EMS或（分子式：见正文）的三元复合物。用Mg2+代替Mn2+的三元复合物可能具有后一种构型。给出了一种对增强数据的新颖处理方法（“高金属”近似法）。

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引用本文的文献

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Structural basis for VO2+ inhibition of nitrogenase activity (A): 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy.VO₂⁺对固氮酶活性抑制的结构基础（A）：通过电子核双共振光谱法确定的³¹P和²³Na与固氮酶铁蛋白核苷酸结合位点处金属的相互作用。
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