Direct electrochemistry of enzymes from the cytochrome P4502C family
Data(s) |
01/04/2005
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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 | |
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 |