In photosystem II (PSII), photosynthetic water oxidation occurs at the tetramanganese-calcium cluster that cycles through light-induced intermediates (S0-S4) to produce oxygen from two substrate waters. The surrounding hydrogen-bonded amino acid residues and waters form channels that facilitate proton transfer and substrate water delivery, thereby ensuring efficient water oxidation. The residue D1-S169 lies in the "narrow" channel and forms hydrogen bonds with the Mn4CaO5 cluster via waters W1 and Wx. To probe the role of the narrow channel in substrate-water binding, we studied the D1-S169A mutation. PSII core complexes isolated from mutant cells exhibit inefficient S-state cycling and delayed oxygen evolution. The S2-state multiline EPR spectrum of D1-S169A PSII core complexes differed significantly from that of wild-type, and FTIR difference spectra showed that the mutation strongly perturbs the extensive network of hydrogen bonds that extends at least from D1-Y161 (YZ) to D1-D61. These results imply a possible role of D1-S169 in proton egress or substrate water delivery.
D1-S169A Substitution of Photosystem II Perturbs Water Oxidation.
Ipsita Ghosh,Gourab Banerjee,Christopher J. Kim,K. Reiss,Victor S. Batista,R. Debus,G. Brudvig
Published 2019 in Biochemistry
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- Publication year
2019
- Venue
Biochemistry
- Publication date
2019-02-01
- Fields of study
Biology, Medicine, Chemistry, Environmental Science
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- Source metadata
Semantic Scholar, PubMed
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