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- W2159733196 abstract "Difference spectra at 77 K of intact Escherichia coli K12 grown under oxygen-limited conditions revealed the presence of cytochrome a 1. In the presence of CO, the band of the reduced form, observed in both the α and λ regions of the spectrum, was decreased. Dualwavelength scanning spectrophotometry at sub-zero temperatures revealed a flash-dissociable CO-binding pigment with a broad band around 595 nm, identified as cytochrome a 1 Photolysis in the presence of O2 revealed no such band in difference spectra where the reference spectrum was that of the CO-liganded form, a result consistent with the binding of O2 to cytochrome a 1. Repeated cycles of photolysis and recombination of the cytochrome with CO were demonstrated at −46 °C. The apparent energy of activation for the reaction with CO was 10·9 kcal mol−1 (45·6 kJ mol−1). The results are discussed in relation to previous assumptions and results regarding ligand binding to cytochrome a 1 and the function of this cytochrome in bacterial respiration." @default.
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- W2159733196 date "1981-08-01" @default.
- W2159733196 modified "2023-09-26" @default.
- W2159733196 title "The Light-reversible Binding of Carbon Monoxide to Cytochrome a1 in Escherichia coli K12" @default.
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- W2159733196 doi "https://doi.org/10.1099/00221287-125-2-431" @default.
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