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

Jane G. DeWitt | Zendy

Open Access

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

Author(s) -

Jane G. DeWitt

Publication year - 1992

Publication title -

osti oai (u.s. department of energy office of scientific and technical information)

Language(s) - English

Resource type - Reports

DOI - 10.2172/7047693

Subject(s) - methane monooxygenase , chemistry , x ray absorption spectroscopy , active center , extended x ray absorption fine structure , absorption (acoustics) , ribonucleotide reductase , absorption spectroscopy , monooxygenase , crystallography , inorganic chemistry , stereochemistry , photochemistry , methane , enzyme , organic chemistry , materials science , biochemistry , physics , cytochrome p450 , quantum mechanics , protein subunit , composite material , gene

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.

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