Authors: Igarashi, Robert Y.; Seefeldt, Lance C.

Source: Critical Reviews in Biochemistry and Molecular Biology, Volume 38, Number 4, July-August 2003 , pp. 351-384(34)

Publisher: Informa Healthcare

Abstract:

This review focuses on recent developments elucidating the mechanism of the Mo-dependent nitrogenase. This enzyme, responsible for the majority of biological nitrogen fixation, is composed of two component proteins called the MoFe protein and the Fe protein. Recent progress in understanding the mechanism of this enzyme has focused on elucidating the structures of the active site metal clusters and of the proteins, understanding substrate interactions with the active site, defining the flow of electron transfer between the metal clusters, and defining the various roles of MgATP hydrolysis.

Keywords: Nitrogen cycle; metalloenzyme; MgATP; electron transfer; FeS cluster

Document Type: Research article

DOI: http://dx.doi.org/10.1080/10409230391036766

Affiliations: 1: Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322, USA

Publication date: 2003-07-01

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