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Photosynthetic water oxidation in Synechocystis sp. PCC6803: mutations D1-E189K, R and Q are without influence on electron transfer at the donor side of photosystem II.

Biochimica et biophysica acta - 1 Nov 2001

Clausen J, Winkler S, Hays A M, Hundelt M, Debus R J, Junge W

Abstract excerpt

The oxygen-evolving manganese cluster (OEC) of photosynthesis is oxidised by the photochemically generated primary oxidant (P(+*)(680)) of photosystem II via a tyrosine residue (Y(Z), Tyr161 on the D1 subunit of Synechocystis sp. PCC6803). The redox span between these components is rather small and probably tuned by protonic equilibria. The very efficient electron transfer from Y(Z) to P(+*)(680) in nanoseconds...

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PMID: 11779556
DOI: 10.1016/s0005-2728(01)00217-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Photosynthetic water oxidation in Synechocystis sp. PCC6803: mutations D1-E189K, R and Q are without influence on electron transfer at the donor side of photosystem II.PMID 11779556Read ↗

Perturbing the water cavity surrounding the manganese cluster by mutating the residue D1-valine 185 has a strong effect on the water oxidation mechanism of photosystem II.Semantic proximity Read ↗

Engineering of an alternative electron transfer path in photosystem II.Semantic proximity Read ↗

The D1-D61N mutation in Synechocystis sp. PCC 6803 allows the observation of pH-sensitive intermediates in the formation and release of O₂ from photosystem II.Semantic proximity Read ↗

Site-directed mutations at D1-Thr179 of photosystem II in Synechocystis sp. PCC 6803 modify the spectroscopic properties of the accessory chlorophyll in the D1-branch of the reaction center.Semantic proximity Read ↗

Engineering of the protein environment around the redox-active TyrZ in photosystem II. The role of F186 and P162 in the D1 protein of Synechocystis 6803.Semantic proximity Read ↗

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Requirement for Asn298 on D1 protein for oxygen evolution: analyses by exhaustive amino acid substitution in the green alga Chlamydomonas reinhardtii.Semantic proximity Read ↗

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Role of Arg180 of the D2 protein in photosystem II structure and function.Semantic proximity Read ↗

D1' centers are less efficient than normal photosystem II centers.Semantic proximity Read ↗

Modulating the redox potential of the stable electron acceptor, Q(B), in mutagenized photosystem II reaction centers.Semantic proximity Read ↗

Phe265 of the D1 protein is required to stabilize plastoquinone binding in the QB-binding site of photosystem II in Synechocystis sp. PCC 6803.Semantic proximity Read ↗

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