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Tyrosines in Biological Electron Transfer (pp.31-56) $100.00
Authors:  (Mariana Voicescu, Petra Hellwig, Laboratoire de Spectroscopie Vibrationnelle et Electrochimie des Biomolécules, UMR 7177, Institut de Chimie, CNRS-Université de Strasbourg, Strasbourg, France, and others)
Specific amino acid side chains are crucial to the stability of proteins structure and in
the catalysis of enzymatic reactions. An important role is granted to Tyr residues and Tyr
derivatives originating from posttranslational modifications. An example for such a
modified Tyr is found in cytochrome c oxidase, where a covalent linkage between a Tyr
and a His was found. The role of this linkage for the catalytic mechanism was explored
by a number of research groups, several of the studies including model compound
studies. Electrochemical and spectroscopic studies gave evidence to the influence of this
linkage on the electron transfer ability of the Tyr and its function within the catalytic

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Tyrosines in Biological Electron Transfer (pp.31-56)