Microencapsulation of Chloroplast Particles
Author(s) -
Masao Kitajima,
Warren L. Butler
Publication year - 1976
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.57.5.746
Subject(s) - ferredoxin , chloroplast , photosystem i , photosystem ii , chemistry , hydrogenase , electron transfer , photosystem , photochemistry , substrate (aquarium) , membrane , oxidoreductase , photosynthesis , biophysics , chromatium , electron transport chain , ferredoxin—nadp(+) reductase , p700 , biochemistry , biology , enzyme , ecology , gene
Chloroplast and photosystem I particles were encapsulated in small spheres (about 20 mum diameter) with an artificial membrane built up by cross-linking amino groups of protamine with toluenediisocyanate. The artificial membrane was permeable to small substrate and product molecules but not to soluble proteins. Photosystem I activity was retained by the encapsulated chloroplast particles. Washed photosystem I particles were encapsulated with the soluble proteins, ferredoxin, and ferredoxin-NADP oxidoreductase, and the microcapsules photoreduced NADP using ascorbate plus dichlorophenolindophenol as the electron donor. The photosystem I particles were also encapsulated with hydrogenase from Chromatium and a very low rate of photoevolution of hydrogen was obtained. The results show that chloroplast membrane fragments can be encapsulated with soluble proteins that couple transfer reactions to the primary photochemical apparatus.
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