Journal
INORGANIC CHEMISTRY
Volume 44, Issue 13, Pages 4546-4554Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ic048794w
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- NCRR NIH HHS [RR-01209] Funding Source: Medline
- NIGMS NIH HHS [GM-32134] Funding Source: Medline
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The diiron active sites of the reduced hydroxylases from methane monooxygenase (MMOHred) and toluene/o-xylene monooxygenase (ToMOH(red)) have been investigated by X-ray absorption spectroscopy (XAS). Results of Fe K-edge and extended X-ray absorption fine structure analysis reveal subtle differences between the hydroxylases that may be correlated to access of the active site. XAS data were also recorded for each hydroxylase in the presence of its respective coupling protein. MMOB affects the outer-shell scattering contributions in the diiron site of MMOHred, whereas ToMOD exerts its main effect on the first-shell ligation of ToMOH(red); it also causes a slight decrease in the Fe-Fe separation. These results provide an initial step toward delineating the differences in structure and reactivity in bacterial multicomponent monooxygenase proteins.
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