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• W2023135802 endingPage "16258" @default.
• W2023135802 startingPage "16247" @default.
• W2023135802 abstract "The reduction potentials of beef heart cytochrome c and cytochromes c2 from Rhodopseudomonas palustris, Rhodobacter sphaeroides, and Rhodobacter capsulatus were measured through direct electrochemistry at a surface-modified gold electrode as a function of temperature in nonisothermal experiments carried out at neutral and alkaline pH values. The thermodynamic parameters for protein reduction (ΔS°rc and ΔH°rc) were determined for the native and alkaline conformers. Enthalpy and entropy terms underlying species-dependent differences in E° and pH- and temperature-induced E° changes for a given cytochrome were analyzed. The difference of about +0.1 V in E° between cytochromes c2 and the eukaryotic species can be separated into an enthalpic term (−ΔΔH°rc/F) of +0.130 V and an entropic term (TΔΔS°rc/F) of −0.040 V. Hence, the higher potential of the bacterial species appears to be determined entirely by a greater enthalpic stabilization of the reduced state. Analogously, the much lower potential of the alkaline conformer(s) as compared to the native species is by far enthalpic in origin for both protein families, and is largely determined by the substitution of Met for Lys in axial heme ligation. Instead, the biphasic E°/temperature profile for the native cytochromes is due to a difference in reduction entropy between the conformers at low and high temperatures. Temperature-dependent 1H NMR experiments suggest that the temperature-induced transition also involves a change in orientation of the axial methionine ligand with respect to the heme plane." @default.
• W2023135802 created "2016-06-24" @default.
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• W2023135802 date "1997-12-01" @default.
• W2023135802 modified "2023-10-02" @default.
• W2023135802 title "Redox Thermodynamics of the Native and Alkaline Forms of Eukaryotic and Bacterial Class I Cytochromes <i>c</i>" @default.
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• W2023135802 doi "https://doi.org/10.1021/bi971535g" @default.
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