Probing the coordination and function of Fe4S4 modules in nitrogenase assembly protein NifB

Lee A. Rettberg; Jarett Wilcoxen; Chi Chung Lee; Martin T. Stiebritz; Kazuki Tanifuji; R. David Britt; Yilin Hu

doi:10.1038/s41467-018-05272-8

Nature Communications (Jul 2018)

Probing the coordination and function of Fe4S4 modules in nitrogenase assembly protein NifB

Lee A. Rettberg,
Jarett Wilcoxen,
Chi Chung Lee,
Martin T. Stiebritz,
Kazuki Tanifuji,
R. David Britt,
Yilin Hu

Affiliations

Lee A. Rettberg: Department of Molecular Biology and Biochemistry, University of California
Jarett Wilcoxen: Department of Chemistry, University of California
Chi Chung Lee: Department of Molecular Biology and Biochemistry, University of California
Martin T. Stiebritz: Department of Molecular Biology and Biochemistry, University of California
Kazuki Tanifuji: Department of Molecular Biology and Biochemistry, University of California
R. David Britt: Department of Chemistry, University of California
Yilin Hu: Department of Molecular Biology and Biochemistry, University of California

DOI: https://doi.org/10.1038/s41467-018-05272-8
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 8

Abstract

Read online

NifB is a key enzyme in the biosynthesis pathway of the nitrogenase FeMo cofactor. Here, the authors investigate the maturation of its iron-sulfur clusters by EPR and biochemical analyses, showing how individual precursor clusters participate in the formation of the final iron-sulfur cluster.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal