AbstractO2 reduction was investigated in photosystem I (PSI) complexes isolated from cyanobacteria Synechocystis sp. PCC 6803 wild type (WT) and menB mutant strain, which is unable to synthesize phylloquinone and contains plastoquinone at the quinone-binding site A1. PSI complexes from WT and menB mutant exhibited different dependencies of O2 reduction on light intensity, namely, the values of O2 reduction rate in WT did not reach saturation at high intensities, in contrast to the values in menB mutant. The obtained results suggest the immediate phylloquinone involvement in the light-induced O2 reduction by PSI
In photosystem I (PSI), phylloquinone participates to electron transfer as secondary electron accept...
Photosystem II (PSII), the water/plastoquinone photo-oxidoreductase, plays a key energy input role i...
In photosystem I (PSI), phylloquinone participates to electron transfer as secondary electron accept...
AbstractO2 reduction was investigated in photosystem I (PSI) complexes isolated from cyanobacteria S...
AbstractIt was found that the contribution of segments of photosynthetic electron transport chain (P...
AbstractPlastoquinol (PQH2-9) and plastoquinone (PQ-9) mediate photosynthetic electron transfer. We ...
Recent evidence has indicated the presence of novel plastoquinone-binding sites, {Q}_C and {Q}_D, in...
Various O2-utilizing electron sinks, including the soluble flavodiiron proteins (Flv1/3), and the me...
AbstractPhotosystem (PS) I preparations from spinach and from a cyanobacterium contain two molecules...
AbstractThe reduction and reoxidation kinetics of the first quinone-type electron acceptor in photos...
AbstractPhotosysthetic cleavage of water molecules to molecular oxygen is a crucial process for all ...
AbstractThe effect of the plastoquionone (PQ) pool oxidation state on minimum chlorophyll fluorescen...
AbstractThe oxidation of the PQ-pool after illumination with 50 or 500μmolquantam−2s−1 was measured ...
Photosynthesis converts solar energy into chemical energy to drive the biological processes of life ...
AbstractThe PsaE protein is located at the reducing side of photosystem I (PSI) and is involved in d...
In photosystem I (PSI), phylloquinone participates to electron transfer as secondary electron accept...
Photosystem II (PSII), the water/plastoquinone photo-oxidoreductase, plays a key energy input role i...
In photosystem I (PSI), phylloquinone participates to electron transfer as secondary electron accept...
AbstractO2 reduction was investigated in photosystem I (PSI) complexes isolated from cyanobacteria S...
AbstractIt was found that the contribution of segments of photosynthetic electron transport chain (P...
AbstractPlastoquinol (PQH2-9) and plastoquinone (PQ-9) mediate photosynthetic electron transfer. We ...
Recent evidence has indicated the presence of novel plastoquinone-binding sites, {Q}_C and {Q}_D, in...
Various O2-utilizing electron sinks, including the soluble flavodiiron proteins (Flv1/3), and the me...
AbstractPhotosystem (PS) I preparations from spinach and from a cyanobacterium contain two molecules...
AbstractThe reduction and reoxidation kinetics of the first quinone-type electron acceptor in photos...
AbstractPhotosysthetic cleavage of water molecules to molecular oxygen is a crucial process for all ...
AbstractThe effect of the plastoquionone (PQ) pool oxidation state on minimum chlorophyll fluorescen...
AbstractThe oxidation of the PQ-pool after illumination with 50 or 500μmolquantam−2s−1 was measured ...
Photosynthesis converts solar energy into chemical energy to drive the biological processes of life ...
AbstractThe PsaE protein is located at the reducing side of photosystem I (PSI) and is involved in d...
In photosystem I (PSI), phylloquinone participates to electron transfer as secondary electron accept...
Photosystem II (PSII), the water/plastoquinone photo-oxidoreductase, plays a key energy input role i...
In photosystem I (PSI), phylloquinone participates to electron transfer as secondary electron accept...