Abstract
Optical studies on Rps. viridis RCs provided evidence that all four hemes of cytochrome c have different absorption spectra in the α-band domain as well as midpoint potentials [1–4]. In this work we used the individual spectra of each heme and linear least-squares method to elucidate the quantity of every heme from full absorption spectra of cytochrome c in the α-band region as function of redox potential. For all four hemes the values of midpoint potentials established by the method of decomposition are in good agreement with those determined earlier [1].
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References
Dracheva, S.M., Drachev, L.A., Konstantinov, A.A., Semenov, A.Yu., Skulachev, V.P., Arutjunjan, A.M., Shuvalov, V.A. and Zaberezhnaya, S.M.(1988) Eur. J. Biochem. 171, 253–264
Alegria G. and Dutton, P.L. (1987) in Cytochrome Systems (Papa, S., Chance, B. and Ernster, L., Eds.) pp 601–608, Plenum Press, New York and London
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Vermeglio, A., Richaud, P. and Breton, J. (1989) FEBS Lett. 243, 259–263
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Dracheva, S.M., Drachev, A.L., Shinkarev, V.P. (1990). The Thermodynamic Characteristic of Four-Heme Cytochrome C from Rhodopseudomonas Viridis Reaction Centers. In: Baltscheffsky, M. (eds) Current Research in Photosynthesis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0511-5_40
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DOI: https://doi.org/10.1007/978-94-009-0511-5_40
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