FTIR study of conformational substates in the CO adduct of cytochrome c oxidase from Rhodobacter sphaeroides

Biochemistry
D MitchellG Ulrich Nienhaus

Abstract

Fourier transform infrared (FTIR) spectroscopy of cytochrome c oxidase from Rhodobacter sphaeroides reveals multiple CO stretch bands that are associated with different conformational substates of the enzyme. Here we report the temperature dependence of the infrared bands for the CO bound to the Fea3 heme iron and to CuB. We have also studied the kinetics of ligand return from Fea3 to CuB using temperature derivative spectroscopy (TDS). Two classes of substates (alpha/beta) can be distinguished from their different properties with regard to the width of the IR band, the temperature dependence of the peak position, and the peak of the enthalpy distribution. The pronounced temperature dependence of the stretch frequencies in the beta conformation and the lack thereof in the alpha conformation implies very different dynamic behavior in the active site and reflects structural differences between the two conformations, most likely a shift of the position of CuB in response to a change in its stereochemical environment. Similar conformational changes will be necessary during the catalytic cycle of the enzyme when dioxygen is bound in the active site.

References

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Citations

Dec 27, 2011·Journal of Inorganic Biochemistry·F MelinJ Weiss
Aug 20, 2014·Biochimica Et Biophysica Acta·Satoru NakashimaTeizo Kitagawa
Mar 6, 2013·Biochimica Et Biophysica Acta·Karin NienhausG Ulrich Nienhaus
Dec 4, 2003·Biophysical Journal·Promod R PratapG Ulrich Nienhaus
Apr 22, 2004·Biochimica Et Biophysica Acta·Olöf Einarsdóttir, Istvan Szundi
Jan 15, 2000·The Journal of Biological Chemistry·S HanD L Rousseau
Dec 25, 2019·Biophysical Journal·Istvan SzundiÓlőf Einarsdóttir

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