Abstract
CO not only bonds hematin iron in blood hemoglobin but also ligands hematin iron atoms of cytochrome a/sub 3/. Nonuniform distribution of CO means that rapidly metabolizing tissue are more susceptible to CO toxicity. Mitochondria are protected by branching and cushioning mechanism so CO toxicity response is not linear as in COHb formation. O/sub 2/ flux in respiratory change is not altered by CO. In these in vitro experiments, as little as 100 ppM CO transiently disrupted cytochrome system in transition from anoxia to nonmoxia, slowing the oxidaton of the chain. Pigeon mitochondria were extremely sensitive to CO when in metabolically-active (uncoupled) state. Increased binding of CO to cytochrome a/sub 3/ during anoxia was observed.
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