X-ray spectroscopic observation of an interstitial carbide in NifEN-bound FeMoco precursor

The iron-molybdenum cofactor (FeMoco) of nitrogenase contains a biologically unprecedented μ(6)-coordinated C(4-) ion. Although the role of this interstitial atom in nitrogenase catalysis is unknown, progress in understanding its biosynthetic origins has been made. Here we report valence-to-core Fe...

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Bibliographic Details
Published in:Journal of the American Chemical Society Vol. 135; no. 2; p. 610
Main Authors: Lancaster, Kyle M, Hu, Yilin, Bergmann, Uwe, Ribbe, Markus W, DeBeer, Serena
Format: Journal Article
Language:English
Published: United States 16.01.2013
Subjects:
Iron Compounds - chemistry
Iron Compounds - metabolism
Molecular Structure
Molybdoferredoxin - chemistry
Molybdoferredoxin - metabolism
Spectrometry, X-Ray Emission
Tricarboxylic Acids - chemistry
ISSN:1520-5126, 1520-5126
Online Access:Get more information
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Summary:The iron-molybdenum cofactor (FeMoco) of nitrogenase contains a biologically unprecedented μ(6)-coordinated C(4-) ion. Although the role of this interstitial atom in nitrogenase catalysis is unknown, progress in understanding its biosynthetic origins has been made. Here we report valence-to-core Fe Kβ X-ray emission spectroscopy data to show that this C(4-) ion is present in the Fe(8)S(9) "L-cluster," which is the immediate precursor to FeMoco prior to the insertion of molybdenum and coordination by homocitrate. These results accord with recent evidence supporting a role for the S-adenosylmethionine-dependent enzyme NifB in the incorporation of carbon into the FeMoco center of nitrogenase.
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ISSN:1520-5126
1520-5126
DOI:10.1021/ja309254g