Evidence that histidine forms a coordination bond to the A(0A) and A(0B) chlorophylls and a second H-bond to the A(1A) and A(1B) phylloquinones in M688H(PsaA) and M668H(PsaB) variants of Synechocystis sp. PCC 6803

Biochim Biophys Acta. 2014 Aug;1837(8):1362-75. doi: 10.1016/j.bbabio.2014.04.004. Epub 2014 Apr 16.

Abstract

The axial ligands of the acceptor chlorophylls, A(0A) and A(0B), in Photosystem I are the Met sulfur atoms of M688(PsaA) and M668(PsaB). To determine the role of the Met, His variants were generated in Synechocystis sp. PCC 6803. Molecular dynamics simulations on M688H(PsaA) show that there exist low energy conformations with the His coordinated to A(0A) and possibly H-bonded to A(1A). Transient EPR studies on M688H(PsaA) indicate a more symmetrical electron spin distribution in the A(1A) phyllosemiquinone ring consistent with the presence of an H-bond to the C1 carbonyl. Ultrafast optical studies on the variants show that the 150fs charge separation between P₇₀₀ and A(0) remains unaffected. Studies on the ns timescale show that 57% of the electrons are transferred from A(0A)(-) to A(1A) in M688H(PsaA) and 48% from A(0B)(-) to A(1B) in M668H(PsaB); the remainder recombine with P₇₀₀(+) with 1/e times of 25ns and 37ns, respectively. Those electrons that reach A(1A) and A(1B) in the branch carrying the mutation are not transferred to FX, but recombine with P₇₀₀(+) with 1/e times of ~15μs and ~5μs, respectively. Hence, the His is coordinated to A0 in all populations, but in a second population, the His may be additionally H-bonded to A(1). Electron transfer from A(0) to A(1) occurs only in the latter, but the higher redox potentials of A(0) and A(1) as a result of the stronger coordination bond to A(0) and the proposed second H-bond to A(1) preclude electron transfer to the Fe/S clusters.

Keywords: A(0); A(1); Chlorophyll a; Photosynthesis; Photosystem I; Phylloquinone.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Chlorophyll / chemistry*
  • Chlorophyll / genetics
  • Chlorophyll / metabolism
  • Electron Spin Resonance Spectroscopy
  • Electron Transport
  • Histidine
  • Hydrogen Bonding
  • Kinetics
  • Ligands
  • Mutation
  • Photosynthesis / genetics*
  • Photosystem I Protein Complex / chemistry*
  • Photosystem I Protein Complex / genetics
  • Synechocystis / chemistry
  • Synechocystis / genetics*
  • Synechocystis / growth & development

Substances

  • Ligands
  • Photosystem I Protein Complex
  • Chlorophyll
  • Histidine