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Fikret Mamedov

Researcher at Uppsala University

Publications -  107
Citations -  3254

Fikret Mamedov is an academic researcher from Uppsala University. The author has contributed to research in topics: Photosystem II & Electron paramagnetic resonance. The author has an hindex of 29, co-authored 107 publications receiving 2763 citations. Previous affiliations of Fikret Mamedov include Technical University of Berlin & Lund University.

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Molecular interference of Cd2+ with Photosystem II

TL;DR: Overall electron transfer and partial electron transfer were studied by a combination of EPR spectroscopy of individual redox components, flash-induced variable fluorescence and steady state oxygen evolution measurements, and both Ca2+ and DCMU abolished Cd2+-induced effects partially and in different sites.
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A five-coordinate Mn( iv ) intermediate in biological water oxidation: spectroscopic signature and a pivot mechanism for water binding

TL;DR: The identification of a unique intermediate in biological water oxidation establishes the water binding mechanism in the S2 to S3 state transition.
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Quantification of photosystem I and II in different parts of the thylakoid membrane from spinach.

TL;DR: The results suggest that PSI in grana margins have two additional light-harvesting complex II (LHCII) trimers per reaction center compared toPSI in stroma lamellae, and that PSII ingrana has four LHCII trimer per monomer compared to PS II in stromae.
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Photodamage of iron-sulphur clusters in photosystem I induces non-photochemical energy dissipation.

TL;DR: It is demonstrated that the iron–sulphur clusters of PSI are more sensitive to high light stress than previously anticipated, but PSI with damaged FeS clusters still functions as a non-photochemical photoprotective energy quencher (PSI-NPQ).
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Dimeric and monomeric organization of photosystem II. Distribution of five distinct complexes in the different domains of the thylakoid membrane.

TL;DR: Steady state electron transfer, flash-induced fluorescence decay, and EPR analysis revealed that nearly all of the dimeric forms represent oxygen-evolving PSII centers, and a large fraction did not evolve oxygen.