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- W1993622307 abstract "Several rate constants for one-electron reduction of cytochrome P450 are more rapid in the absence than in the presence of the specific substrate. The respective values for methyl viologen, nicotinamide adenine dinucleotide and the 1-methyl-4-(and -3-)carbamidopyridinium radicals are 2.6, 3.4, 6 and 35 × 107 M−1 s−1 without camphor, and 0.15, 0.1, 1.8 and 110 × 107 M−1 s−1 for the camphor complex. Hydrated electrons react with cytochrome P450 with a rate constant of 3.0 × 1010 M−1 s−1 whether camphor is bound or not, but little of the reduction takes place at the haem iron. No reduction of the haem iron by CO2•- or O2•- could be detected, whether camphor is bound or not." @default.
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- W1993622307 date "1979-02-01" @default.
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- W1993622307 title "Electron transfer from pyridinyl radicals, hydrated electrons, CO2•- and O2•- bacterial cytochrome P450" @default.
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- W1993622307 doi "https://doi.org/10.1016/0006-291x(79)90210-9" @default.
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