Pyridine and imidazole reversibly inhibit the respiratory burst in porcine and human neutrophils: evidence for the involvement of cytochrome b558 in the reaction.
Heterocyclic nitrogenous bases, such as pyridine and imidazole which bind to heme-iron in cytochromes, inhibited the respiratory burst in intact neutrophils and NADPH-dependent oxygen consumption in lysed cells. Inhibition was accompanied by a spectral change in reduced cytochrome b558 as judged by low-temperature spectroscopy at 77 K. The position and shape of the alpha-band of the cytochrome were significantly altered upon exposure to pyridine or some other bases. Both inhibition and spectral changes were reversible. The results are consistent with the view that cytochrome b558 is involved in the NADPH oxidase system in neutrophils.
D000818:Animals; D003080:Cold Temperature; D003573:Cytochrome b Group / Q000378:metabolism*; D006801:Humans; D007093:Imidazoles / Q000494:pharmacology*; D009249:NADP / Q000378:metabolism; D019255:NADPH Oxidases; D009504:Neutrophils / Q000187:drug effects* / Q000378:metabolism; D010101:Oxygen Consumption / Q000187:drug effects*; D011725:Pyridines / Q000494:pharmacology*; D013053:Spectrophotometry; D013552:Swine
D003573:Cytochrome b Group; D007093:Imidazoles; D011725:Pyridines; D009249:NADP; C029899:imidazole; C036888:cytochrome b558; D019255:NADPH Oxidases; C023666:pyridine