Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1503, Issue 1-2, Pages 246-259Publisher
ELSEVIER
DOI: 10.1016/S0005-2728(00)00228-0
Keywords
proton-coupled electron transfer; photosystem II; water oxidation; redox active tyrosine
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According to current estimates, the photosynthetic water oxidase functions with a quite restricted driving force. This emphasizes the importance of the catalytic mechanisms in this enzyme. The general problem of coupling electron and proton transfer is discussed from this viewpoint and it is argued that 'weak coupling' is preferable to 'strong coupling'. Weak coupling can be achieved by facilitating deprotonation either before (proton-first path) or after (electron-first path) the oxidation step. The proton-first path is probably relevant to the oxidation of tyrosine Y-Z by P-680. Histidine D1-190 is believed to play a key role as a proton acceptor facilitating Y-Z deprotonation. The pK(a) of an efficient proton acceptor is submitted to conflicting requirements, since a high pK(a) favors proton transfer from the donor, but also from the medium. H-bonding between Y-Z and His, together with the Coulombic interaction between negative tyrosinate and positive imidazolium, are suggested to play a decisive role in alleviating these constraints. Current data and concepts on the coupling of electron and proton transfer in the water oxidase are discussed. (C) 2001 Elsevier Science B.V. All rights reserved.
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