Direct electrochemistry of the enzyme, methylamine dehydrogenase, from bacterium W3A1.
The electrochemical response of methylamine dehydrogenase from bacterium W3A1 at edge-plane-oriented pyrolytic graphite (epg) and modified gold electrodes has been investigated. Quasi-reversible electron transfer has been observed. Variations in concentration of different cations and anions gave rise to both promotion and inhibition of the direct response. A catalytic response of the enzyme in the presence of methylamine has been observed at both an epg electrode and a 2,2'-dithiodiglycolic-acid-modified gold electrode surface, and the effects of various cations and anions on the catalytic peak current have been investigated. The spectroelectrochemical results obtained at an optically transparent thin-layer electrode, modified with 2,2'-dithiodiglycolic acid, are also reported. In the presence of 1,1'-dimethylferrocene-3-(1-ethanol-2-amine) (14.8 microM), the results reveal a midpoint potential of -148 mV for methylamine dehydrogenase from bacterium W3A1. This is in very close agreement to the value obtained in the cyclic voltammetric investigations of -140 mV.
Burrows
A L
AL
Inorganic Chemical Laboratory, University of Oxford, England.
Hill
H A
HA
Leese
T A
TA
Mcintire
W S
WS
Nakayama
H
H
Sanghera
G S
GS
D000838:Anions; D001419:Bacteria / Q000201:enzymology*; D002384:Catalysis; D002412:Cations; D004563:Electrochemistry; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry*; D013379:Substrate Specificity
D000838:Anions; D002412:Cations; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors