The versatile enzyme system nitrogenase accomplishes the challenging reduction of N2and other substrates through the use of two main metalloclusters. For molybdenum nitrogenase, the catalytic component NifDK contains the [Fe8S7]-core P-cluster and a [MoFe7S9C-homocitrate] cofactor called the M-cluster. These chemically unprecedented metalloclusters play a critical role in the reduction of N2, and both originate from [Fe4S4] clusters produced by the actions of NifS and NifU. Maturation of P-cluster begins with a pair of these [Fe4S4] clusters on NifDK called the P*-cluster. An accessory protein NifZ aids in P-cluster fusion, and reductive coupling is facilitated by NifH in a stepwise manner to form P-cluster on each half of NifDK. For M-cluster biosynthesis, two [Fe4S4] clusters on NifB are coupled with a carbon atom in a radical-SAM dependent process, and concomitant addition of a ‘ninth’ sulfur atom generates the [Fe8S9C]-core L-cluster. On the scaffold protein NifEN, L-cluster is matured to M-cluster by the addition of Mo and homocitrate provided by NifH. Finally, matured M-cluster in NifEN is directly transferred to NifDK, where a conformational change locks the cofactor in place. Mechanistic insights into these fascinating biosynthetic processes are detailed in this chapter.
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May 2017
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A His6 motif of the human calprotectin heterodimer with a bound Mn(II) ion. In this issue of Essays in Biochemistry, Neumann et al. look at the how pathogenic Neisseria species exploit host metaloproteins, such as calprotectin, to acquire essential transition metal ions. For further details, see pages 211-223. Image kindly provided by Elizabeth M. Nolan (Massachusetts Institute of Technology). - PDF Icon PDF LinkTable of Contents
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Review Article|
May 09 2017
Cluster assembly in nitrogenase
Nathaniel S. Sickerman;
Nathaniel S. Sickerman
1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, U.S.A.
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Lee A. Rettberg;
Lee A. Rettberg
1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, U.S.A.
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Chi Chung Lee;
Chi Chung Lee
1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, U.S.A.
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Yilin Hu;
1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, U.S.A.
Correspondence: Yilin Hu (yilinh@uci.edu) or Markus W. Ribbe (mribbe@uci.edu)
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Markus W. Ribbe
1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, U.S.A.
2Department of Chemistry, University of California, Irvine, CA 92697-3900, U.S.A.
Correspondence: Yilin Hu (yilinh@uci.edu) or Markus W. Ribbe (mribbe@uci.edu)
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Publisher: Portland Press Ltd
Received:
December 13 2016
Revision Received:
February 23 2017
Accepted:
March 01 2017
Online ISSN: 1744-1358
Print ISSN: 0071-1365
© 2017 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2017
Essays Biochem (2017) 61 (2): 271–279.
Article history
Received:
December 13 2016
Revision Received:
February 23 2017
Accepted:
March 01 2017
Citation
Stephen J. Lippard, Jeremy M. Berg, Nathaniel S. Sickerman, Lee A. Rettberg, Chi Chung Lee, Yilin Hu, Markus W. Ribbe; Cluster assembly in nitrogenase. Essays Biochem 9 May 2017; 61 (2): 271–279. doi: https://doi.org/10.1042/EBC20160071
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