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How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation.

ABSTRACT: During the process of biological nitrogen fixation, the enzyme nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein; the Fe protein mediates the coupling of ATP hydrolysis to interprotein electron transfer, whereas the active site of the MoFe protein contains the polynuclear FeMo cofactor, a species composed of seven iron atoms, one molybdenum atom, nine sulfur atoms, an interstitial light atom, and one homocitrate molecule. This Perspective provides an overview of biological nitrogen fixation and introduces three contributions to this special feature that address central aspects of the mechanism and assembly of nitrogenase.

SUBMITTER: Howard JB

PROVIDER: S-EPMC1859894 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

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How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation.

Howard James B JB Rees Douglas C DC

Proceedings of the National Academy of Sciences of the United States of America 20061106 46

During the process of biological nitrogen fixation, the enzyme nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein; the Fe protein mediates the coupling of ATP hydrolysis to interprotein electron transfer, whereas the active site of the MoFe protein contains the polynuclear FeMo cofactor, a species composed of seven iron atoms, one molybdenum atom, nine sulf ...[more]

PMID: 17088547

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