Thermodynamic volume cycles for electron transfer in the cytochrome c oxidase and for the binding of cytochrome c to cytochrome c oxidase

Biophysical Journal
J A KornblattP C Kahn

Abstract

Dilatometry is a sensitive technique for measuring volume changes occurring during a chemical reaction. We applied it to the reduction-oxidation cycle of cytochrome c oxidase, and to the binding of cytochrome c to the oxidase. We measured the volume changes that occur during the interconversion of oxidase intermediates. The numerical values of these volume changes have allowed the construction of a thermodynamic cycle that includes many of the redox intermediates. The system volume for each of the intermediates is different. We suggest that these differences arise by two mechanisms that are not mutually exclusive: intermediates in the catalytic cycle could be hydrated to different extents, and/or small voids in the protein could open and close. Based on our experience with osmotic stress, we believe that at least a portion of the volume changes represent the obligatory movement of solvent into and out of the oxidase during the combined electron and proton transfer process. The volume changes associated with the binding of cytochrome c to cytochrome c oxidase have been studied as a function of the redox state of the two proteins. The volume changes determined by dilatometry are large and negative. The data indicate quite clearly...Continue Reading

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Citations

May 2, 2002·Biochimica Et Biophysica Acta·Jack A Kornblatt, M Judith Kornblatt
Feb 28, 2003·European Journal of Biochemistry·Jack A KornblattMichael C Marden
Dec 1, 2014·Advances in Colloid and Interface Science·Albert SanfeldAnnie Steinchen
Jun 27, 2000·Biophysical Journal·D P Kharakoz
Jul 7, 2007·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Karen M Black, Carmichael J A Wallace
Dec 8, 2020·Current Opinion in Structural Biology·Samantha S Stadmiller, Gary J Pielak

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