Document Detail

X-ray spectroscopic observation of an interstitial carbide in NifEN-bound FeMoco precursor.
MedLine Citation:
PMID:  23276198     Owner:  NLM     Status:  MEDLINE    
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.
Kyle M Lancaster; Yilin Hu; Uwe Bergmann; Markus W Ribbe; Serena DeBeer
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2013-01-08
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  135     ISSN:  1520-5126     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-16     Completed Date:  2013-06-19     Revised Date:  2014-01-23    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  610-2     Citation Subset:  IM    
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MeSH Terms
Iron Compounds / chemistry*,  metabolism
Molecular Structure
Molybdoferredoxin / chemistry*,  metabolism
Spectrometry, X-Ray Emission
Tricarboxylic Acids / chemistry
Grant Support
Reg. No./Substance:
0/Iron Compounds; 0/Molybdoferredoxin; 0/NifB cofactor; 0/Tricarboxylic Acids; 3562-74-1/homocitric acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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