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D1-S169A Substitution of Photosystem II Perturbs Water Oxidation

Journal Article · · Biochemistry
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. Finally, these results imply a possible role of D1-S169 in proton egress or substrate water delivery.
Research Organization:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). National Energy Research Scientific Computing Center (NERSC)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Grant/Contract Number:
FG02-05ER15646; SC0001423; SC0005291
OSTI ID:
1530435
Journal Information:
Biochemistry, Journal Name: Biochemistry Journal Issue: 10 Vol. 58; ISSN 0006-2960
Publisher:
American Chemical Society (ACS)Copyright Statement
Country of Publication:
United States
Language:
English

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