Formation and characterization of a transition state complex of Azotobacter vinelandii nitrogenase

被引：54

作者：

Duyvis, MG ^{[1
]}

Wassink, H ^{[1
]}

Haaker, H ^{[1
]}

机构：

[1] AGR UNIV WAGENINGEN,DEPT BIOCHEM,6703 HA WAGENINGEN,NETHERLANDS

来源：

FEBS LETTERS | 1996年 / 380卷 / 03期

关键词：

nitrogenase (Azotobacter vinelandii); ATP-analogue; aluminium fluoride; molecular switch protein;

D O I：

10.1016/0014-5793(96)00019-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A stable complex is formed between the nitrogenase proteins of Azotobacter vinelandii, aluminium fluoride and MgADP. All nitrogenase activities are inhibited. The complex formation was found to be reversible. An incubation at 50 degrees C recovers nitrogenase activity. The complex has been characterized with respect to protein and nucleotide composition and redox state of the metal-sulphur clusters. Based on the inhibition by aluminium fluoride together with MgADP, it is proposed that a stable transition state complex of nitrogenase is isolated.

引用

页码：233 / 236

页数：4

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