Single crystal EXAFS of nitrogenase

Single crystal EXAFS of nitrogenase

Single crystals of the nitrogenase Mo-Fe protein have been examined by polarized x-ray absorption spectroscopy. For different orientations, the Mo-Fe amplitude of the Mo K-edge EXAFS was found to change by a factor of 2.5, whereas the Mo-S component varied by only +- 15%. The orientation dependence...

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Veröffentlicht in:J. Am. Chem. Soc.; (United States) 1986-03, Vol.108 (5), p.1049-1055
Hauptverfasser: Flank, A. M, Weininger, M, Mortenson, L. E, Cramer, S. P
Format: Artikel
Sprache:eng
Schlagworte:
400301 - Organic Chemistry- Chemical & Physicochemical Properties- (-1987)
Biological and medical sciences
CRYSTAL STRUCTURE
Crystalline structure
CRYSTALS
DATA
ELEMENTS
ENZYMES
EXPERIMENTAL DATA
Fundamental and applied biological sciences. Psychology
INFORMATION
INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY
IRON
METALS
Molecular biophysics
MOLYBDENUM
MONOCRYSTALS
NITRO-GROUP DEHYDROGENASES
NITROGENASE
NONMETALS
NUMERICAL DATA
OXIDOREDUCTASES
SPECTROSCOPY
Structure in molecular biology
SULFUR
TRANSITION ELEMENTS
X-RAY SPECTROSCOPY
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Beschreibung
Zusammenfassung:Single crystals of the nitrogenase Mo-Fe protein have been examined by polarized x-ray absorption spectroscopy. For different orientations, the Mo-Fe amplitude of the Mo K-edge EXAFS was found to change by a factor of 2.5, whereas the Mo-S component varied by only +- 15%. The orientation dependence of the EXAFS spectra has been used to investigate the geometry and orientation of the Mo, Fe, S clusters within the Mo-Fe protein. This represents the first application of single-crystal EXAFS to an enzyme of unknown crystal structure. 38 references, 10 figures, 3 tables.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja00265a034