DINITROGEN REDUCTION BY NITROGENASE - IF N2 ISNT BROKEN, IT CANT BE FIXED

被引：17

作者：

REES, DC

机构：

[1] DC Rees, California Institute of Technology, Division of Chemistry and Chemical Engineering, Pasadena, CA 91125

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1993年 / 3卷 / 06期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

D O I：

10.1016/0959-440X(93)90157-G

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：

Nitrogenase consists of two component metalloproteins, the iron protein and molybdenum-iron protein, which together catalyze the ATP-dependent reduction of dinitrogen to ammonia during biological nitrogen fixation. With the recent crystal structure determinations of both proteins, a structural framework is now available for interpreting the mechanism of nitrogenase at the molecular level.

引用

页码：921 / 928

页数：8

共 41 条

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