Direct electrochemistry of the hydroxylase of soluble methane monooxygenase from Methylococcus capsulatus (Bath).
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.
Inorganic Chemistry Laboratory, University of Oxford, UK.
J
J
Kazlauskaite
H A
HA
Hill
P C
PC
Wilkins
H
H
Dalton
D004563:Electrochemistry; D004566:Electrodes; D008772:Methylococcaceae / Q000201:enzymology*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000737:chemistry*; D012995:Solubility
D010105:Oxygenases; C021555:methane monooxygenase