NifB-dependent in vitro synthesis of the iron-molybdenum cofactor of nitrogenase

被引：78

作者：

Curatti, L ^{[1
]}

Ludden, PW ^{[1
]}

Rubio, LM ^{[1
]}

机构：

[1] Univ Calif Berkeley, Dept Plant & Microbial Biol, Berkeley, CA 94720 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2006年 / 103卷 / 14期

关键词：

iron-sulfur; S-adenosylmethionine radical;

D O I：

10.1073/pnas.0601115103

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Biological nitrogen fixation, an essential process of the biogeochemical nitrogen cycle that supports life on Earth, is catalyzed by the nitrogenase enzyme. The nitrogenase active site contains an iron and molybdenum cofactor (FeMo-co) composed of 7Fe-9S-Mohomocitrate and one not-yet-identified atom, which probably is the most complex [Fe-S] cluster in nature. Here, we show the in vitro synthesis of FeMo-co from its simple constituents, Fe, S, Mo, and homocitrate. The in vitro FeMo-co synthesis requires purified NifB and depends on S-adenosylmethionine, indicating that radical chemistry is required during FeMo-co assembly.

引用

页码：5297 / 5301

页数：5

共 34 条

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