Radical SAM-dependent Formation of a Nitrogenase Cofactor Core on NifB

Overview

Journal J Inorg Biochem

Specialty Biochemistry

Date 2022 May 13

PMID 35550498

Authors

Yiling A Liu

Robert Quechol

Joseph B Solomon

Chi Chung Lee

Markus W Ribbe

Yilin Hu

Britt Hedman

Keith O Hodgson

Affiliations

Soon will be listed here.

Abstract

Nitrogenase is a versatile metalloenzyme that reduces N, CO and CO at its cofactor site. Designated the M-cluster, this complex cofactor has a composition of [(R-homocitrate)MoFeSC], and it is assembled through the generation of a unique [FeSC] core prior to the insertion of Mo and homocitrate. NifB is a radical S-adenosyl-L-methionine (SAM) enzyme that is essential for nitrogenase cofactor assembly. This review focuses on the recent work that sheds light on the role of NifB in the formation of the [FeSC] core of the nitrogenase cofactor, highlighting the structure, function and mechanism of this unique radical SAM methyltransferase.

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