Electrochemical aspects of cytochrome P-450 system from liver microsomes

The electrochemical behaviour of microsomal and partially purified rabbit liver cytochrome P-450 was studied with the aim to simplify the enzyme system. The following results were obtained: 1. Electrochemically regenerated NADPH has an activity of about 30 % compared to the regeneration by glucose-6...

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Bibliographic Details
Published in:Bioelectrochemistry and Bioenergetics 1977, Vol.4 (4), p.500-507
Main Authors: Scheller, F., Renneberg, R., Strnad, G., Pommerening, K., Mohr, P.
Format: Article
Language:English
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Summary:The electrochemical behaviour of microsomal and partially purified rabbit liver cytochrome P-450 was studied with the aim to simplify the enzyme system. The following results were obtained: 1. Electrochemically regenerated NADPH has an activity of about 30 % compared to the regeneration by glucose-6-phosphate dehydrogenase. 2. Solubilized cytochrome P-450 shows a polarographic reduction step at —580 mV vs. the S.C.E. and was partially reduced, in contrast to microsomal P-450, which was not reducible. 3. Cathodically reduced oxygen as well as added H 2O 2 support demethylation and hydroxylation of various substrates in the absence of NADPH. The reaction rate does not depend on the electrode surface area at constant current. The cathodic reduction of oxygen is the most convenient form of the substitution of the cofactor and reductase because the cathodic reduction and the enzymatic reaction proceed in parallel.
ISSN:0302-4598
DOI:10.1016/0302-4598(77)80048-2