A HIGHLY RESOLVED, OXYGEN-EVOLVING PHOTOSYSTEM-II PREPARATION FROM SPINACH THYLAKOID MEMBRANES - ELECTRON-PARAMAGNETIC-RES AND ELECTRON-TRANSPORT PROPERTIES
A HIGHLY RESOLVED, OXYGEN-EVOLVING PHOTOSYSTEM-II PREPARATION FROM SPINACH THYLAKOID MEMBRANES - ELECTRON-PARAMAGNETIC-RES AND ELECTRON-TRANSPORT PROPERTIES
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DOI:
10.1016/0014-5793(81)80608-4
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发表时间:
1981-01-01
期刊:
影响因子:
3.5
通讯作者:
YOCUM, CF
中科院分区:
文献类型:
--
作者:
BERTHOLD, DA;BABCOCK, GT;YOCUM, CF
Photosystem II of chloroplast thylakoid membranes provides light-generated oxidizing equivalents which ultimately oxidize water to oxygen. The system is known to contain a reaction center chlorophyll complex, P680, a quinone acceptor denoted as Q, a P680 donor molecule designated as Z and a highpotential cytochrome b-559 [l]. The relationship between these components and the presumed manganese protein thought to be the actual site of watersplitting is as yet poorly understood. Attempts to resolve this photoreaction from intact membranes of higher plant chloroplasts by detergent action have resulted in a variety of preparations ranging from reaction centers [2, 3] to more complex assemblies with vesicular structure [3]. While these preparations are generally able to support electron transfer from an added donor to an exogenous acceptor, all higher plant preparations reported are unable to carry out oxygen evolution with high activity. Photosystem II may be isolated from membranes of the cyanobacterium Phormidium laminosum [4]. These preparations, in contrast to those from higher plants, retain high rates of oxygen evolution [4] and are enriched in EPR signal II with residual contamination from PS I, as shown by the presence of some signal I (P700’)[5]. membranes; here we report the properties of oxygenevolving PS II preparations obtained by detergent resolution of chloroplast thylakoid membranes.