X-ray absorption spectroscopic studies of the dinuclear iron center in methane monooxygenase and the sulfure and chlorine centers in photographic materials

Technical Report · Mon Nov 30 23:00:00 EST 1992

DOI:https://doi.org/10.2172/7047693· OSTI ID:7047693

DeWitt, J G

The dinuclear iron center of the hydroxylase component of soluble methane monooxygenase (MMO) from Methylococcus capsulatus and Methylosinus trichosporiwn has been studied by X-ray absorption spectroscopy. Analysis of the Fe K-edge EXAFS revealed that the first shell coordination of the Fe(HI)Fe(IH) oxidized state of the hydroxylase from M. capsulatus consists of approximately 6 N and 0 atoms at an average distance of 2.04 [Angstrom]. The Fe-Fe distance was determined to be 3.4 [Angstrom]. 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 MMO is significantly different from the active sites of the dinuclear iron proteins hemery and ribonucleotide reductase. In addition, the results of the first shell fits suggest that there are more oxygen than nitrogen donor ligands.

• Research Organization: Stanford Linear Accelerator Center, Menlo Park, CA (United States)
• Sponsoring Organization: DOE; USDOE, Washington, DC (United States)
• DOE Contract Number: AC03-76SF00515
• OSTI ID: 7047693
• Report Number(s): SLAC-410; SLAC/SSRL--0003; ON: DE93008625
• Country of Publication: United States
• Language: English

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