Cytochrome Systems pp 657-666 | Cite as
Isolation of the Photosystem Two Reaction Centre and the Location and Function of Cytochrome b-559
Abstract
Although there have been numerous studies to understand the role of cytochrome b-559 in photosynthesis, no clear picture has yet emerged. The study of this cytochrome is complicated by the fact that there seems to be two distinctly different pools. One pool consists of a low potential form (E~ −30 mV) and is located in the unappressed stromal regions of higher plant chloroplasts (1). This low potential form may be in some way linked to electron and proton translocation through the cytochrome b6-f complex (2). The other pool is localized in the appressed regions which constitute the grana (3,4) and normally seems to exist in a high potential form (E~ 380 mV). In the earlier literature there was some confusion about the redox properties of the high potential form because its midpoint potential can be significantly modified after certain treatments which affect membrane structure especially by the action of detergents (5,6). In this case the Em changes from 380 mV to about 80 mV. Apparently this shift is due to a perturbation of the environment around the cytochrome and can be reversed by adding back polar lipids derived from the thylakoid, particularly digalactosyldiacylglycerol (7,8). Reconstitution of a certain extrinsic polypeptide (23 kDa) associated with water oxidation, has also been reported to revert the cytochrome to its high potential form (9).
Keywords
Methyl Viologen Water Oxidation Membrane Fragment High Plant Chloroplast Extrinsic PolypeptidePreview
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References
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