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

Technical Report · Tue Dec 01 00:00:00 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: SLAC National Accelerator Lab., Menlo Park, CA (United States)
• Sponsoring Organization: USDOE; USDOE, Washington, DC (United States)
• DOE Contract Number: AC03-76SF00515
• OSTI ID: 7047693
• Report Number(s): SLAC-410; SLAC/SSRL-0003; ON: DE93008625
• Resource Relation: Other Information: Thesis (Ph.D.)
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
OXYGENASES
PROTEIN STRUCTURE
X-RAY SPECTROSCOPY
ENZYMES
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PROTEINS
SPECTROSCOPY
090900* - Biomass Fuels- Processing- (1990-)
550200 - Biochemistry
400101 - Activation
Nuclear Reaction
Radiometric & Radiochemical Procedures