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Title: Assembly scaffold NifEN: A structural and functional homolog of the nitrogenase catalytic component

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America
 [1];  [2];  [1];  [1];  [3];  [4];  [2];  [1]
  1. Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900,
  2. Department of Chemistry, Stanford University, Stanford, CA 94305,
  3. Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900,, Department of Chemistry, University of California, Irvine, CA 92697-2025,
  4. Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center, Stanford University, Menlo Park, CA 94025

Significance This work provides direct evidence for the formation of an M-cluster on the assembly scaffold NifEN, establishing NifEN as the second known protein that houses a nitrogenase cofactor. A “half-on, half-off” scheme of cofactor biosynthesis can be proposed based on the outcome of this study, which suggests an asymmetric nature of the assembly sites in the seemingly equivalent αβ-halves of NifEN and a coordination of various biosynthetic events via a unique conformational switch on/off mechanism. The comparable substrate-reducing capabilities of NifEN and NifDK establish the former as a structural and functional homolog of the latter, providing a proof-of-concept for the feasibility of probing key catalytic features of NifDK via reconstruction of a NifDK equivalent on the basis of a “simplified” template, NifEN.

Sponsoring Organization:
USDOE
Grant/Contract Number:
AC02-76SF00515
OSTI ID:
1288984
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Vol. 113 Journal Issue: 34; ISSN 0027-8424
Publisher:
Proceedings of the National Academy of SciencesCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 17 works
Citation information provided by
Web of Science

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