D1-D2 complex of the photosystem II reaction center from spinach. Isolation and partial characterization.
A pigment-protein complex consisting of D1 and D2 proteins, but depleted in the two lower molecular mass components of photosystem II, i.e. cytochrome b-559 and psbI gene product, has been isolated by octyl-beta-D-glucopyranoside treatment of the purified photosystem II reaction center complex from spinach [(1987) Proc. Natl. Acad. Sci. USA 84, 109-112], followed by separation by high performance liquid chromatography using a gel-permeation column (TSK G3000 SW). The isolated complex is photochemically active in the photoreduction of intrinsic pheophytin a under steady-state illumination, in the presence of dithionite and methyl viologen, and exhibits pigment stoichiometries similar to those in the untreated reaction center, indicating that the D1-D2 complex provides the site of primary photochemistry in photosystem II, as well as the principal binding sites of pigments in the reaction center.
Tang
X S
XS
Department of Biology, Faculty of Science, Okayama University, Japan.
Fushimi
K
K
Satoh
K
K
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008027:Light; D046911:Macromolecular Substances; D008970:Molecular Weight; D045322:Photosynthetic Reaction Center Complex Proteins / Q000302:isolation & purification* / Q000378:metabolism; D045332:Photosystem II Protein Complex; D010944:Plants / Q000378:metabolism*; D013053:Spectrophotometry
D046911:Macromolecular Substances; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex