Open AccessDirect Electrochemistry of the Hydroxylase of Soluble Methane Monooxygenase from Methylococcus Capsulatus (Bath)
Author(s) -
Kazlauskaite Jurate,
Hill H. Allen O.,
Wilkins Patricia C.,
Dalton Howard
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.00552.x
Subject(s) - chemistry , methane monooxygenase , redox , titration , saturated calomel electrode , electrochemistry , inorganic chemistry , redox titration , electrode , enzyme , biochemistry , reference electrode
The redox properties of the hydroxylase component of soluble methane monooxygenase from Methylococcus cupsulutus (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. capsulutus (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.