[Microsomal hemoprotein reduction by superoxide radical formed on NADPH-specific flavoprotein].
The superoxide radicals formed on NADPH-specific flavoprotein of liver microsomes can reduce cytochromes c, b5, and P-450. This reaction is inhibited under aerobic conditions by a low molecular weight analog of superoxide dismutase, e.g. the copper-tyrosine complex. The inhibitory effect of the complex is not observed under anaerobic conditions. Based on the results obtained a scheme of the electron transfer between the flavoprotein and haemoproteins involving superoxide radicals is proposed.
D000332:Aerobiosis; D000818:Animals; D003580:Cytochromes / Q000378:metabolism*; D005420:Flavoproteins / Q000378:metabolism*; D007700:Kinetics; D008862:Microsomes, Liver / Q000378:metabolism*; D009249:NADP; D010084:Oxidation-Reduction; D010100:Oxygen; D051381:Rats; D013481:Superoxides
D003580:Cytochromes; D005420:Flavoproteins; D013481:Superoxides; D009249:NADP; D010100:Oxygen
Vosstanovlenie mikrosomal'nykh gemoproteidov superokisnym radikalom, obrazuiushchimsia na NADPH-spetsifichnom flavoproteide.