Summary
The energy cost of introduction of charges into regions of low dielectric strength in proteins can be reduced by associated binding of a proton to appropriately placed residues. Such protonations can be important in peroxidases and other soluble proteins, and are likely to be central to the protonmotive mechanism of oxidases. Three residues in subunit I of cytochrome oxidase that are likely to interfere with such protonations have been examined by mutagenesis, and the data are discussed in the light of the known crystal structures.
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© 1998 Springer-Verlag Tokyo
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Rich, P.R., Meunier, B., Jünemann, S. (1998). Coupling of Ion and Charge Movements: From Peroxidases to Protonmotive Oxidases. In: Ishimura, Y., Shimada, H., Suematsu, M. (eds) Oxygen Homeostasis and Its Dynamics. Keio University Symposia for Life Science and Medicine, vol 1. Springer, Tokyo. https://doi.org/10.1007/978-4-431-68476-3_5
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DOI: https://doi.org/10.1007/978-4-431-68476-3_5
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