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Abstract

The green algae Chlamydomonas reinhardii has developed a system to separate hydrogen and oxygen evolution in time with the endogenous substrate as intermediates. In this report the pathway of reducing equivalents from the endogenous substrate to photosystem I (and hydrogenase) and the properties of photosystem II in oxygen evolution and the essential peptide components have been studied. The two systems are the components for a two-compartment system of a chloroplast battery in which oxygen and hydrogen evolution is to be separated in space. A respiratory NADH dehydrogenase coupled to plastoquinone and the cytochrome b-6/f-complex of the photosynthetic system is described here. By studies in vivo, in cell free systems, thylakoid membranes and at the enzyme level the properties of the system have been characterized. Evidence has been collected to support the hypothesis formulated by P. Bennoun that the studied enzyme is part of a chlororespiratory system of the algae Chlamydomonas that may be converted to hydrogen evolution. The photosystem II preparation of Chlamydomonas has been studied in function and in peptide composition. In particular the functional role of certain integral peptides have been studied with photo-affinity labeled inhibitors.

Additional information

Authors: GODDE D, RUHR-UNIVERSITAT BOCHUM (GERMANY);NEUMANN E, RUHR-UNIVERSITAT BOCHUM (GERMANY);TREBST A RUHR-UNIVERSITAT BOCHUM (GERMANY), RUHR-UNIVERSITAT BOCHUM (GERMANY)
Bibliographic Reference: EUR 9530 EN (1984) MF, 47 P., BFR 120, BLOW-UP COPY BFR 235, EUROFFICE, LUXEMBOURG, POB 1003
Availability: Can be ordered online
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