X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron-molybdenum cofactor

Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the ide...

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Vydané v:Science (American Association for the Advancement of Science) Ročník 334; číslo 6058; s. 974
Hlavní autori: Lancaster, Kyle M, Roemelt, Michael, Ettenhuber, Patrick, Hu, Yilin, Ribbe, Markus W, Neese, Frank, Bergmann, Uwe, DeBeer, Serena
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 18.11.2011
Predmet:
Azotobacter vinelandii - chemistry
Biocatalysis
Carbon - chemistry
Ligands
Models, Molecular
Molecular Structure
Molybdoferredoxin - chemistry
Molybdoferredoxin - metabolism
Nitrogen - chemistry
Oxidation-Reduction
Oxygen - chemistry
Spectrometry, X-Ray Emission
ISSN:1095-9203, 1095-9203
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Shrnutí:Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient nifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C(4-). Identification of the central atom will drive further studies on its role in catalysis.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1095-9203
1095-9203
DOI:10.1126/science.1206445