Radical SAM-dependent formation of a nitrogenase cofactor core on NifB

Yiling A Liu; Robert Quechol; Joseph B Solomon; Chi Chung Lee; Markus W Ribbe; Yilin Hu; Britt Hedman; Keith O Hodgson

doi:10.1016/j.jinorgbio.2022.111837

Radical SAM-dependent formation of a nitrogenase cofactor core on NifB

J Inorg Biochem. 2022 Aug:233:111837. doi: 10.1016/j.jinorgbio.2022.111837. Epub 2022 Apr 20.

Authors

Yiling A Liu¹, Robert Quechol¹, Joseph B Solomon², Chi Chung Lee¹, Markus W Ribbe³, Yilin Hu⁴, Britt Hedman⁵, Keith O Hodgson⁶

Affiliations

¹ Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States of America.
² Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States of America; Department of Chemistry, University of California, Irvine, CA 92697-2025, United States of America.
³ Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States of America; Department of Chemistry, University of California, Irvine, CA 92697-2025, United States of America. Electronic address: mribbe@uci.edu.
⁴ Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States of America. Electronic address: yilinh@uci.edu.
⁵ Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States of America. Electronic address: bhedman@stanford.edu.
⁶ Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States of America; Department of Chemistry, Stanford University, Stanford, CA 94305, United States of America. Electronic address: hodgsonk@stanford.edu.

Abstract

Nitrogenase is a versatile metalloenzyme that reduces N₂, CO and CO₂ at its cofactor site. Designated the M-cluster, this complex cofactor has a composition of [(R-homocitrate)MoFe₇S₉C], and it is assembled through the generation of a unique [Fe₈S₉C] 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 [Fe₈S₉C] core of the nitrogenase cofactor, highlighting the structure, function and mechanism of this unique radical SAM methyltransferase.

Keywords: Biosynthesis; FeS cluster; M-cluster; NifB; Nitrogenase; Radical SAM enzyme.

Publication types

Review
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Metalloproteins*
Methyltransferases
Molybdoferredoxin / chemistry
Nitrogenase* / chemistry
S-Adenosylmethionine / chemistry

Substances

Metalloproteins
Molybdoferredoxin
S-Adenosylmethionine
Nitrogenase
Methyltransferases

Abstract

Publication types

MeSH terms

Substances

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