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• W2079189084 abstract "The isolation and purification of cytochrome c 550 from the methylamine‐oxidizing electron‐transport chain in Thiobacillus versutus is reported. The cytochrome is a single‐heme‐containing type I cytochrome c with a relative molecular mass of 16 ± 1 kDa, an isoelectric point of 4.6 ± 0.1, a midpoint potential of 272 ± 3 mV at pH < 4 and 255 ± 5 mV at pH = 7.0, and an axial coordination of the Fe by a methionine and a histidine. The midpoint potential decreases with increasing pH due to the deprotonation of a group tentatively identified as a propionate (p K a = 6.5 ± 0.1 and 6.7 ± 0.1 in the oxidized and reduced protein, respectively) and a change in the Fe coordination at pH > 10. The electron‐self‐exchange rate appears to depend strongly on the ionic strength of the solution and is relatively insensitive to changes in pH. At 313 K and pH 5.2 the electron‐exchange rate amounts to 0.7 × 10 2 M −1 s −1 and 5.3 × 10 2 M −1 s −1 at I = 40 mM and I = 200 mM, respectively. Amino acid composition and molar absorption coefficients at various wavelengths are reported. Resonances of heme protons and the ±H 3 group of the ligand methionine of the Fe have been identified in the 1 H‐NMR spectrum of the reduced as well as the oxidized cytochrome." @default.
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• W2079189084 date "1990-09-01" @default.
• W2079189084 modified "2023-10-03" @default.
• W2079189084 title "Isolation and characterization of cytochrome c550 from the methylamine-oxidizing electron-transport chain of Thiobacillus versutus" @default.
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• W2079189084 doi "https://doi.org/10.1111/j.1432-1033.1990.tb19272.x" @default.
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