Bicarbonate rescues damaged proton-transfer pathway in photosystem II

Gourab Banerjee, Ipsita Ghosh, Christopher J. Kim, Richard J. Debus, Gary W. Brudvig

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


The membrane-protein complex photosystem II (PSII) catalyzes photosynthetic water oxidation. Proton transfer plays an integral role in the catalytic cycle of water oxidation by maintaining charge balance to regulate and ensure the efficiency of the process. The hydrogen-bonded amino-acid residues that surround the oxygen-evolving complex (OEC) provide an efficient pathway for proton removal. Hence, it is crucial to identify these pathways to provide deeper insights into the proton-transfer mechanisms. In this study, we have used bicarbonate as a mobile exogenous proton-transfer reagent to recover the activity lost by site-directed mutations in order to identify amino-acid residues participating in the proton-transfer pathway. We find that bicarbonate restores efficient S-state cycling in D2-K317A PSII core complexes, but not in D1-D61A and CP43-R357K PSII core complexes, indicating that bicarbonate chemical rescue can be used to differentiate single-point mutations affecting the pathways of proton transfer from mutations that affect other aspects of the water-oxidation mechanism.

Original languageEnglish
Pages (from-to)611-617
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number8
Publication statusPublished - Aug 1 2019


  • Bicarbonate
  • Oxygen evolution
  • Photosystem II
  • Proton transfer
  • Water oxidation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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