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The Alkaline Conformational Equilibria of Cytochrome C Studied by Resonance Raman Spectroscopy

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Spectroscopy of Biological Molecules: Modern Trends
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Abstract

The heme protein cytochrome c (Cyt) serves as an electron carrier in the respiratory chain of aerobic organism [1]. In alkaline solutions, the ferric Cyt exhibits pH-dependent equilibria including conformational transitions which have been suggested to be related with those occuring during the physiological redox process with cytochrome c oxidase (CcO). In this work, we have studied these conformational equilibria of Cyt by resonance Raman (RR) spectroscopy.

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References

  1. Wilson, M.T., and Greenwood, C. (1996) in Cytochrome c: A Multidisciplinary Approach, Scott, R.A., Mauk, A.G. Eds., University Science Books: Mill Valley, 1996, 611–634.

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  4. Döpner, S., Hildebrandt, P., Mauk, A.G., Lenk, H. and Stemple, W. (1996) Analysis of Vibrational Spectra of Multicomponent Systems. Application to pH-Dependent Resonance Raman Spectra of Ferricytochrome c, Spectrochim. Acta 51A, 573–584.

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© 1997 Springer Science+Business Media Dordrecht

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Döpner, S., Hildebrandt, P., Rosell, F.I., Mauk, A.G. (1997). The Alkaline Conformational Equilibria of Cytochrome C Studied by Resonance Raman Spectroscopy. In: Carmona, P., Navarro, R., Hernanz, A. (eds) Spectroscopy of Biological Molecules: Modern Trends. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5622-6_37

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  • DOI: https://doi.org/10.1007/978-94-011-5622-6_37

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6369-2

  • Online ISBN: 978-94-011-5622-6

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