Spectroelectrochemistry of cytochrome P450cam.

Article Details


Bistolas N, Christenson A, Ruzgas T, Jung C, Scheller FW, Wollenberger U

Spectroelectrochemistry of cytochrome P450cam.

Biochem Biophys Res Commun. 2004 Feb 13;314(3):810-6.

PubMed ID
14741708 [ View in PubMed

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 (E(0')) 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.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
MetyraponeCamphor 5-monooxygenaseProteinPseudomonas putida