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The bidirectional hydrogenase of Synechocystis sp. PCC 6803 works as an electron valve during photosynthesis

Appel, Jens, Phunpruch, Saranya, Steinmüller, Klaus, Schulz, Rüdiger
Archives of microbiology 2000 v.173 no.5-6 pp. 333-338
Synechocystis, active sites, electron transfer, electrons, ferredoxin hydrogenase, fluorescence, genes, light intensity, mutants, oxidation, oxygen, photosystem I, photosystem II
The activity of the bidirectional hydrogenase of the cyanobacterium Synechocystis sp. PCC 6803 was found not to be regulated in parallel to respiration but to photosynthesis. A mutant with a deletion in the large hydrogenase subunit gene (hoxH), which contains the active site, was impaired in the oxidation of photosystem I (PSI) when illuminated with light, which excites either PSI alone or both photosystems. The fluorescence of photosystem II (PSII) of this mutant was higher than that of wild-type cells. The transcript level of the photosynthetic genes psbA, psaA and petB was found to be different in the hydrogenase-free mutant cells compared to wild-type cells, which indicates that the hydrogenase has an effect on the regulation of these genes. Collectively, these results suggest that the bidirectional hydrogenase functions as a valve for low-potential electrons generated during the light reaction of photosynthesis, thus preventing a slowing down of electron transport. This conclusion is supported by growth curves demonstrating that the mutant cells need more time to adapt to changing light intensities. Investigations of the wild-type and ΔhoxH strains strongly suggest that Synechocystis contains only the bidirectional hydrogenase, which seems to be essentially insensitive to oxygen.