Direct electrochemistry of enzymes from the cytochrome P4502C family


Autoria(s): Shukla, Alka; Gillam, Elizabeth M.; Mitchell, Deanne J.; Bernhardt, Paul V.
Data(s)

01/04/2005

Resumo

The human cytochromes P450 are responsible for the clearance of similar to 90% of xenobiotics yet comparatively little is known about their electrochemistry. Here we report the first direct electrochemistry of P450s from the 2C subfamily; one of the major groups of enzymes from this family. Specifically, the proteins that we have examined are recombinant human P450s 2C9, 2C 18 and 2C 19 and reversible Fe-III/II couples are seen in the absence of dioxygen. Even in the presence of trace amounts of dioxygen, a pronounced cathodic response is seen which is assigned to catalytic reduction of the bound dioxygen ligand by the ferrous P450. (c) 2005 Elsevier B.V. All rights reserved.

Identificador

http://espace.library.uq.edu.au/view/UQ:76165

Idioma(s)

eng

Publicador

Elsevier Science Inc

Palavras-Chave #Cytochrome P450 #Voltammetry #Direct Electron Transfer #Electrochemistry #Electron-transfer #Crystal-structure #Escherichia-coli #Resolution #P450(cam) #Binding #Substrate #Metabolism #Protein #Films #C1 #250405 Sensor (Chemical and Bio-) Technology #270108 Enzymes #780105 Biological sciences
Tipo

Journal Article