Efficient oxygenic photosynthesis not only requires synchronous turover and operation of photosystem I (PS I) and photosystem II (PS II) but also the preferential turnover of PS I for cyclic photophosphorylation to maintain required ATP and NADPH ratio during carbon dioxide reduction. Ohe initial higher rate of turnover of PS IIin viva is accounted by the fact that (i) PS I contains only about one-third of total chlorophylls, (ii) about 90% of light harvesting a/b protein (LAC) which accounts for about 50% of the total chlorophylls, remains associated with PS II as PS II-LHC II complexes (PS IIα and (iii) the ratio of PS II/PS I is always greater than unity, in the range of 1–2 : 1 under different environmental regimes. Ohe initial preferential feeding of PS II, due to its larger antenna, is bound to result in faster rate of turn over of PS II than PS I, leading to higher rate of reduction of an intersystem carrier than the rate of its oxidation by PS I. Ohe light dependent phosphorylation of a ‘mobile’ and small pool (−20%) of LHC II of PS IIα (possibly located at the edge of appressed regions of the membranes) increases the repulsive forces of LHC II resulting in its migration to non-appressed region associating itself with PS 1. Ohe phosphorylation itself is controlled by the redox state of an intermediate of electron transport.
Several experimental approaches have provided evidence which suggest that (i) phosphorylation of LAC II involves interaction of cyt b5-f complex with LAC II kinase and the interaction of QA with cyt b5-f complex and (ii) different kinases may be involved in phosphorylation of LHC IIversus PS II polypeptides. Ohe major purpose of light dependent LAC II phosphorylation and its consequent migration close to PS I appears to balance the rate of cyclicversus non-cyclic photophosphorylation. Ohe mechanism by which cyt b5-f complex controls the activation of LAC II is not known. Ohe role of membrane bound ealmodulin, electron transfer through cyt b6-f complex in activation of LAC II kinase should be explored.
Volume 45, 2020
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