Direct electrochemistry of the hydroxylase of soluble methane monooxygenase from Methylococcus capsulatus (Bath)
UNSPECIFIED. (1996) Direct electrochemistry of the hydroxylase of soluble methane monooxygenase from Methylococcus capsulatus (Bath). EUROPEAN JOURNAL OF BIOCHEMISTRY, 241 (2). pp. 552-556. ISSN 0014-2956Full text not available from this repository.
The redox properties of the hydroxylase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath) have been thoroughly investigated. Previous studies used redox indicator titrations and spectroscopic methods for the determination of the concentrations of reduced species. Herein we report, for the first time, direct electrochemistry (i.e. without the use of mediators) of the diiron centers of the hydroxylase from M. capsulatus (Bath) at a modified gold electrode giving rise to two waves at 4(+/-10) mV and -386(+/-14) mV versus saturated calomel electrode (SCE). In addition, the effects of proteins B and B' on the redox reactions were determined. The redox potentials of the complex with protein B are -25(+/-14) mV and -433(+/-8) mV versus SCE whereas protein B' had no effect though it did alter the effect of protein B on the redox potentials.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||EUROPEAN JOURNAL OF BIOCHEMISTRY|
|Date:||15 October 1996|
|Number of Pages:||5|
|Page Range:||pp. 552-556|
Actions (login required)