Regulation of function of proteins by phosphorylation of constituent amino acids has been
studied most extensively in enzymes from mammalian cell and tissue extracts. In 1956 …

Part of the chlL gene encoding a component involved in light-independent
protochlorophyllide reduction was deleted in wild type and in a photosystem I-less strain of …

In the process Of photosynthesis, light is absorbed by various pigments (chlorophylls,
carotenoids, and phycobilins), and light energy is used for the initiation of a chain of redox …

Mutants of the cyanobacterium Synechocystis sp. PCC 6803 have been generated in which
parts of psbC (the gene encoding the Photosystem II chlorophyll-protein CP43) have been …

Ten strains from a collection of mutants of Synechocystis 6803 defective in Photosystem II
(PS II) function were transformed with chromosomal DNA of wild-type and mutant cells …

Two large, hydrophobic polypeptides termed PSI-A and PSI-B of Photosystem I are thought,
as a heterodimer, to harbor all redox centers and pigments required for primary charge …

Cyanobacteria are model organisms for the analysis of photosynthetic processes, nitrogen
fixation and circadian rhythm. Genetic characterization and manipulation of cyanobacteria is …

The photosystem II reaction center can be considered as a water-plastoquinone oxido-
reductase. Using four photons it transfers four electrons from two molecules of water to …

Publisher Summary Quite a range of spectroscopic techniques has been applied to the
characterization of photosystem II (PSII) mutants. These have been applied to whole cells …

Cytochrome b-559 is an integral protein of the photosystem II (PSII) reaction center from both
plants and cyanobacteria. Cytochrome b-559 has the unique structure of a heme crosslinked …