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Spectroelectrochemistry of cytochrome P450cam

Item Type:Article
Title:Spectroelectrochemistry of cytochrome P450cam
Creators Name:Bistolas, N. and Christenson, A. and Ruzgas, T. and Jung, C. and Scheller, F.W. and Wollenberger, U.
Abstract:The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4′-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV-visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4′-dithiodipyridin and dithionite modified electrodes. A formal potential (E0′) of -373mV vs Ag/AgCl 1M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis.
Keywords:Cytochrome P450cam, Dithionite, Modified Electrode, Spectroelectrochemsitry
Source:Biochemical and Biophysical Research Communications
Publisher:Academic Press (U.S.A.)
Page Range:810-816
Date:13 February 2004
Official Publication:https://doi.org/10.1016/j.bbrc.2003.12.159
PubMed:View item in PubMed

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