X-Ray Absorption Spectroscopic Studies of the Dinuclear Iron Center in Methane Monooxygenase and the Sulfure and Chlorine Centers in Photographic Materials
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States); Stanford Univ., CA (United States)
The dinuclear iron center of the hydroxylase component of soluble methane monooxygenase (MMO) from Methylococcus capsulatus (Bath) and Methylosinus trichosproium (OB3b) has been studied by X-ray absorption spectroscopy. Analysis of the Fe K-edge EXAFS revealed that the first shell coordination of the Fe(III)Fe(III) oxidized state of the hydroxylase from M. capsulatus (Bath) consists of approximately 6 N and O atoms at an average distance of 2.04 Å. No evidence for the presence of a short oxo bridge in the iron center of the oxidized hydroxylase was found, suggesting that the active site of the MMO is significantly different from the active sites of the dinuclear iron proteins hemerytherin and ribonucleotide reductase. In addition, the results of the first shell fits suggest that there are more oxygen than nitrogen donor ligands.
- Research Organization:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States); Stanford Univ., CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC)
- DOE Contract Number:
- AC02-76SF00515
- OSTI ID:
- 1454092
- Report Number(s):
- SLAC-R--410; SLAC--410
- Country of Publication:
- United States
- Language:
- English
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X-ray absorption spectroscopic studies of the dinuclear iron center in methane monooxygenase and the sulfure and chlorine centers in photographic materials
X-ray absorption spectroscopic studies of the dinuclear iron center in methane monooxygenase and the sulfur and chlorine centers in photographic materials