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• W2067389266 abstract "In Hydrogenobacter thermophilus cytochrome c552, an electrostatic interaction between Lys8 and Glu68 in the N- and C-terminal helices, respectively, stabilizes its protein structure [Travaglini-Allocatelli, C., Gianni, S., Dubey, V. K., Borgia, A., Di Matteo, A., Bonivento, D., Cutruzzola, F., Bren, K. L., and Brunori, M. (2005) J. Biol. Chem. 280, 25729−25734], this electrostatic interaction being a highly conserved structural feature of the cytochrome c family. In the present study, the functional consequences of removal of the interaction through replacement of Lys8 by Ala have been investigated in order to elucidate the molecular mechanisms responsible for functional control of the protein. The mutation resulted in a decrease in protein stability, as reflected in lowering of the denaturation temperature by ∼2−9 °C, and a negative shift by ∼8 mV of the redox potential (Em) of the protein. The decrease in the protein stability was attributed to the enthalpic loss due to the removal of the intramolecular interaction. The negative shift of the Em value was shown to be due to the effect of the mutation on the entropic contribution to the Em value. The small, but subtle, effects of removal of the conserved electrostatic interaction, occurring at ∼1.4 nm away from heme iron, on the thermodynamic properties of the protein demonstrated not only that the interaction is important for maintaining the functional properties of the protein but also that amino acid residues relatively remote from the heme active site play sizable roles in functional control of the protein." @default.
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• W2067389266 date "2009-12-08" @default.
• W2067389266 modified "2023-10-08" @default.
• W2067389266 title "Role of a Highly Conserved Electrostatic Interaction on the Surface of Cytochrome <i>c</i> in Control of the Redox Function" @default.
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• W2067389266 doi "https://doi.org/10.1021/bi901484b" @default.
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