Abstract
Cytochrome c 552 (Cyt-c 552) is a soluble heme protein which acts as an electron carrier in the respiratory chain of the eubacterium Thermus thermophilus [1]. Cyt-c 552 does not exhibit a lysine-rich domain on the protein surface that in related type-c cytochromes serves for binding to the natural redox partners. This structural pecularity suggests that the molecular interactions with the terminal ba 3 oxidase and, hence, the mechanism of the interprotein electron transfer are qualitatively different compared to the mitochondrial redox couple cytochrome c — cytochrome c oxidase.
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Lecomte, S., Hildebrandt, P., Soulimane, T. (1999). The electron transfer dynamics of cytochrome c 552 from Thermus thermophilus probed by time-resolved surface enhanced resonance Raman spectroscopy. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_45
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DOI: https://doi.org/10.1007/978-94-011-4479-7_45
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