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• W4281550135 endingPage "148570" @default.
• W4281550135 startingPage "148570" @default.
• W4281550135 abstract "Post-translational modifications and naturally occurring mutations of cytochrome c have been recognized as a regulatory mechanism to control its biology. In this work, we investigate the effect of such in vivo chemical modifications of human cytochrome c on its redox properties in the adsorbed state onto an electrode. In particular, tyrosines 48 and 97 have been replaced by the non-canonical amino acid p-carboxymethyl-L-phenylalanine (pCMF), thus mimicking tyrosine phosphorylation. Additionally, tyrosine 48 has been replaced by a histidine producing the natural Y48H pathogenic mutant. Thermodynamics and kinetics of the interfacial electron transfer of wild-type cytochrome c and herein produced variants, adsorbed electrostatically under different local interfacial electric fields, were determined by means of variable temperature cyclic film voltammetry. It is shown that non-native cytochrome c variants immobilized under a low interfacial electric field display redox thermodynamics and kinetics similar to those of wild-type cytochrome c. However, upon increasing the strength of the electric field, the redox thermodynamics and kinetics of the modified proteins markedly differ from those of the wild-type species. The mutations promote stabilization of the oxidized form and a significant increase in the activation enthalpy values that can be ascribed to a subtle distortion of the heme cofactor and/or difference of the amino acid rearrangements rather than to a coarse protein structural change. Overall, these results point to a combined effect of the single point mutations at positions 48 and 97 and the strength of electrostatic binding on the regulatory mechanism of mitochondrial membrane activity, when acting as a redox shuttle protein." @default.
• W4281550135 created "2022-05-27" @default.
• W4281550135 creator A5023014264 @default.
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• W4281550135 date "2022-10-01" @default.
• W4281550135 modified "2023-10-18" @default.
• W4281550135 title "Electric field-induced functional changes in electrode-immobilized mutant species of human cytochrome c" @default.
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• W4281550135 doi "https://doi.org/10.1016/j.bbabio.2022.148570" @default.
• W4281550135 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35643148" @default.
• W4281550135 hasPublicationYear "2022" @default.
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