Thermoluminescence evidence for light-induced oxidation of tyrosine and histidine residues in manganese-depleted photosystem II particles

FEBS Lett. 1992 Feb 3;297(1-2):51-4. doi: 10.1016/0014-5793(92)80325-b.

Abstract

In the thermoluminescence (TL) glow curve of photosystem II, particles depleted of manganese, a tyrosine modifier, 7-chloro-4-nitrobenz-2-oxa-1,3-diazole (NBD) abolishes the TL band appearing around -55 degrees C (TL-55). Addition of a histidine modifier, diethylpyrocarbonate results in the disappearance of the band peaking around -30 degrees C (TL-30). NBD treatment also abolishes the EPR signal IIfast of oxidized tyrosine donor, Yz, and inhibits the electron transport from diphenylcarbazide to 2,6-dichlorophenol-indophenol. It is concluded that the TL-55 and TL-30 bands can be assigned to oxidized tyrosine (Yz+) and histidine (His+) residues, respectively, which participate in electron transfer from manganese to the reaction center of chlorophyll, P680+.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 4-Chloro-7-nitrobenzofurazan / chemistry
  • Diethyl Pyrocarbonate / chemistry
  • Electron Transport
  • Histidine / metabolism*
  • Light*
  • Light-Harvesting Protein Complexes
  • Luminescence
  • Manganese / metabolism*
  • Oxidation-Reduction
  • Photosynthetic Reaction Center Complex Proteins / metabolism*
  • Photosystem II Protein Complex
  • Tyrosine / metabolism*

Substances

  • Light-Harvesting Protein Complexes
  • Photosynthetic Reaction Center Complex Proteins
  • Photosystem II Protein Complex
  • Tyrosine
  • Manganese
  • Histidine
  • 4-Chloro-7-nitrobenzofurazan
  • Diethyl Pyrocarbonate