Function of redox-active tyrosine in photosystem II

Biophys J. 2006 Jun 1;90(11):3886-96. doi: 10.1529/biophysj.105.076984. Epub 2006 Mar 2.

Abstract

Water oxidation at photosystem II Mn-cluster is mediated by the redox-active tyrosine Y(Z). We calculated the redox potential (E(m)) of Y(Z) and its symmetrical counterpart Y(D), by solving the linearized Poisson-Boltzmann equation. The calculated E(m)(Y( )/Y(-)) were +926 mV/+694 mV for Y(Z)/Y(D) with the Mn-cluster in S2 state. Together with the asymmetric position of the Mn-cluster relative to Y(Z/D), differences in H-bond network between Y(Z) (Y(Z)/D1-His(190)/D1-Asn(298)) and Y(D) (Y(D)/D2-His(189)/D2-Arg(294)/CP47-Glu(364)) are crucial for E(m)(Y(Z/D)). When D1-His(190) is protonated, corresponding to a thermally activated state, the calculated E(m)(Y(Z)) was +1216 mV, which is as high as the E(m) for P(D1/D2). We observed deprotonation at CP43-Arg(357) upon S-state transition, which may suggest its involvement in the proton exit pathway. E(m)(Y(D)) was affected by formation of P(D2)(+) (but not P(D1)(+)) and sensitive to the protonation state of D2-Arg(180). This points to an electrostatic link between Y(D) and P(D2).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Manganese / chemistry
  • Mathematics
  • Models, Molecular*
  • Oxidation-Reduction
  • Photosystem II Protein Complex / chemistry*
  • Protons
  • Static Electricity
  • Thermodynamics
  • Tyrosine / chemistry*
  • Water / chemistry

Substances

  • Photosystem II Protein Complex
  • Protons
  • Water
  • Tyrosine
  • Manganese