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- W2077201291 abstract "Abstract Sulfide is both an inhibitor and a slow reductant of oxidized cytochrome c oxidase. When the enzyme is exposed to sulfide for short times (one minute or less) and frozen, the resultant electron paramagnetic resonance (EPR) signals show clearly: low spin heme a, low spin heme a3, the usual “EPR detectable” Cu2+ signal (g⊥ = 2.17, g⊥ = 2.03), and a new Cu2+ signal superimposed on the same region, with (g⊥ ∼ 2.19, g⊥ = 2.05). This new signal presumably arises because the antiferromagnetic coupling postulated to exist between the iron atom of heme a3 and this copper is disrupted when heme a3 is driven to a low spin state by sulfide. The implications of this result with respect to models of the O2-binding site and redox geometry of oxidase are briefly discussed." @default.
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- W2077201291 date "1977-09-01" @default.
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- W2077201291 title "An EPR signal from the “invisible” copper of cytochrome oxidase" @default.
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- W2077201291 doi "https://doi.org/10.1016/0006-291x(77)90244-3" @default.
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