Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor

The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon specie...

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Published inScience (American Association for the Advancement of Science) Vol. 334; no. 6058; p. 940
Main Authors Spatzal, Thomas, Aksoyoglu, Müge, Zhang, Limei, Andrade, Susana L. A., Schleicher, Erik, Weber, Stefan, Rees, Douglas C., Einsle, Oliver
Format Journal Article
LanguageEnglish
Published Washington, DC American Association for the Advancement of Science 18.11.2011
The American Association for the Advancement of Science
Subjects
Atoms
Azotobacter vinelandii - chemistry
Biological and medical sciences
BREVIA
Carbon
Carbon - chemistry
Catalysis
Crystalline structure
Crystallography, X-Ray
Electron Spin Resonance Spectroscopy
Evidence
Fundamental and applied biological sciences. Psychology
Isotopic labeling
Models, Molecular
Molecular biophysics
Molecular Structure
Molybdoferredoxin - chemistry
Nitrogen
Nitrogen - chemistry
Structure in molecular biology
Oxidoreductases
Enzyme
Cofactor
Nitrogenase
Active site
Crystalline structure
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Summary:The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon species.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1214025