Mutation of a metal ligand stabilizes the high-spin form of the S2 state in the O2-producing Mn4CaO5 cluster of photosystem II

Photosynth Res. 2023 Jun;156(3):309-314. doi: 10.1007/s11120-023-00998-z. Epub 2023 Jan 18.

Abstract

The residue D1-D170 bridges Mn4 with the Ca ion in the O2-evolving Mn4CaO5 cluster of Photosystem II. Recently, the D1-D170E mutation was shown to substantially alter the Sn+1-minus-Sn FTIR difference spectra [Debus RJ (2021) Biochemistry 60:3841-3855]. The mutation was proposed to alter the equilibrium between different Jahn-Teller conformers of the S1 state such that (i) a different S1 state conformer is stabilized in D1-D170E than in wild-type and (ii) the S1 to S2 transition in D1-D170E produces a high-spin form of the S2 state rather than the low-spin form that is produced in wild-type. In this study, we employed EPR spectroscopy to test if a high-spin form of the S2 state is formed preferentially in D1-D170E PSII. Our data show that illumination of dark-adapted D1-D170E PSII core complexes does indeed produce a high-spin form of the S2 state rather than the low-spin multiline form that is produced in wild-type. This observation provides further experimental support for a change in the equilibrium between S state conformers in both the S1 and S2 states in a site-directed mutant that retains substantial O2 evolving activity.

Keywords: EPR spectroscopy; FTIR spectroscopy; Oxygen evolution; Photosystem II.

MeSH terms

  • Electron Spin Resonance Spectroscopy
  • Ligands
  • Manganese* / chemistry
  • Mutation
  • Oxidation-Reduction
  • Oxygen / chemistry
  • Photosystem II Protein Complex* / metabolism

Substances

  • Photosystem II Protein Complex
  • Ligands
  • Manganese
  • Oxygen