Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent O2- . generating oxidase from human neutrophils.
The resolved flavoprotein and cytochrome b559 components of the NADPH dependent O2- . generating oxidase from human neutrophils were the subject of further study. The resolved flavoprotein, depleted of cytochrome b559, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent O2- . generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b559, depleted of flavoprotein, demonstrated no measureable NADPH dependent O2- . generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome b559 was rapidly oxidized by oxygen, as was the cytochrome b559 in the intact oxidase.
D000332:Aerobiosis; D000693:Anaerobiosis; D003573:Cytochrome b Group / Q000097:blood* / Q000302:isolation & purification; D005420:Flavoproteins / Q000097:blood* / Q000302:isolation & purification; D006801:Humans; D007700:Kinetics; D009247:NADH, NADPH Oxidoreductases / Q000097:blood* / Q000302:isolation & purification; D019255:NADPH Oxidases; D009504:Neutrophils / Q000201:enzymology*; D013050:Spectrometry, Fluorescence
D003573:Cytochrome b Group; D005420:Flavoproteins; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases; C022709:superoxide-forming enzyme