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• W2506162667 endingPage "655" @default.
• W2506162667 startingPage "631" @default.
• W2506162667 abstract "Cytochrome f is bound to the cytochrome b 6 f complex embedded in the thylakoid membrane, but plastocyanin is a small protein that diffuses between cytochrome f and photosystem I in the thylakoid lumen. The essential feature of electron transfer from cytochrome f to plastocyanin is that a weak, transient complex is formed so as to allow both rapid formation of the reaction complex, and rapid dissociation of products. The reaction has been studied with the proteins in solution, using preparations of the large, heme-containing luminal domain of cytochrome f, by kinetic methods, NMR and computer simulation. The reaction sites have been identified as small areas of hydrophobic residues on the surface immediately above the heme or Cu atom and including ligand residues (Tyr1 for cytochrome f and His87 for plant plastocyanin). A model of the reaction has been developed in which an intermediate encounter complex is formed covering a relatively large area of the surface and serving the purpose of steering the proteins towards a reactive configuration. With plant and algal proteins the main attractive force forming the encounter complex is electrostatic, but the reactive complex depends on desolvation energy to which electrostatics can make little contribution. With cyanobacterial proteins there is considerable species variation. Hydrophobic attraction plays a significant role in formation of the encounter complex as well as the reaction complex and sometimes may dominate. NMR relaxation studies and Brownian dynamics simulations suggest that rather than a single reaction complex, several (encounter) configurations contribute to k et. There are additional features governing the reaction in vivo. Plastocyanin diffuses within the tight luminal space which forms a sheet no more than about 10 nm thick, obstructed by the large luminal domains of photosystem II and other complexes. Solution studies with added viscogens suggest that other soluble luminal proteins would cause little inhibition. The lumen is now thought to expand in the light, contrary to previous evidence, raising the intriguing possibility that expansion and contraction of the thylakoid lumen is a significant method of regulation of electron transport. The role of electrostatic attraction in vivo has been tested with Chlamydomonas mutants. The surprising result was that charge neutralisation had very little effect on either cell growth or the rate of oxidation of cytochrome f, suggesting that the dominant attraction forming the encounter complex in vivo is probably hydrophobic in all oxygenic organisms." @default.
• W2506162667 created "2016-08-23" @default.
• W2506162667 creator A5044532377 @default.
• W2506162667 creator A5085708645 @default.
• W2506162667 date "2016-01-01" @default.
• W2506162667 modified "2023-09-23" @default.
• W2506162667 title "The Interaction Between Cytochrome f and Plastocyanin or Cytochrome c 6" @default.
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