THYLAKOIDS FROM PEA-SEEDLINGS GROWN UNDER INTERMITTENT LIGHT - BIOCHEMICAL AND FLASH-SPECTROPHOTOMETRIC PROPERTIES

Autor(en): JAHNS, P
JUNGE, W 
Stichwörter: A/B-BINDING PROTEINS; ABSORPTION-CHANGE; Biochemistry & Molecular Biology; CHLOROPHYLL-B; ELECTRON-TRANSPORT; HIGHER-PLANTS; MEMBRANES; PHOTOSYNTHETIC WATER OXIDATION; PHOTOSYSTEM-II PREPARATION; PROTON-PUMPING ACTIVITY; SHORT-CIRCUIT
Erscheinungsdatum: 1992
Herausgeber: AMER CHEMICAL SOC
Journal: BIOCHEMISTRY
Volumen: 31
Ausgabe: 32
Startseite: 7390
Seitenende: 7397
Zusammenfassung: 
Thylakoid membranes were isolated from pea seedlings grown under intermittent light (2-min light/118-min dark cycles). These preparations differed from controls (thylakoids from plants grown under 16-h light/8-h dark cycles) in the following respects: 15 times smaller chlorophyll/protein ratio, 10 times greater chlorophyll a/b ratio, absence of light-harvesting chlorophyll a/b binding proteins, and 2-3-fold greater ratio of photosystem II over photosystem I. In addition we found the following: (1) Electrogenic electron transfer around cytochrome b6/f under flashing light was greatly enhanced, probably as a consequence of the greater photosystem II/photosystem I ratio. (2) The rate of proton uptake from the medium at the acceptor side of photosystem II was enhanced, probably by unshielding of the quinone binding domain. (3) The N,N'-dicyclohexylcarbodiimide sensitivity of the proton-pumping activity of photosystem II was absent, which was consistent with the attribution of a N,N'-dicyclohexylcarbodiimide-induced protonic short circuit to chlorophyll a/b binding proteins. (4) The sensitivity of oxygen evolution under continuous light to variations of pH or the concentration of Ca2+ was altered. Chlorophyll a/b binding proteins serve as light-harvesting antennas. We found in addition that they modulated the activity of water oxidation and, in particular, the protolytic reactions around photosystem II.
ISSN: 00062960
DOI: 10.1021/bi00147a025

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