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The cytochrome f –plastocyanin complex as a model to study transient interactions between redox proteins
Author(s) -
Cruz-Gallardo Isabel,
Díaz-Moreno Irene,
Díaz-Quintana Antonio,
De la Rosa Miguel A.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.08.035
Subject(s) - plastocyanin , cytochrome b6f complex , redox , electron transport chain , cytochrome , electron transfer , cytochrome f , chemistry , photosystem i , transient (computer programming) , biophysics , microsecond , cytochrome c1 , cytochrome c , photosynthesis , photosystem ii , photochemistry , coenzyme q – cytochrome c reductase , biochemistry , mitochondrion , biology , enzyme , computer science , physics , organic chemistry , astronomy , operating system
Transient complexes, with a lifetime ranging between microseconds and seconds, are essential for biochemical reactions requiring a fast turnover. That is the case of the interactions between proteins engaged in electron transfer reactions, which are involved in relevant physiological processes such as respiration and photosynthesis. In the latter, the copper protein plastocyanin acts as a soluble carrier transferring electrons between the two membrane‐embedded complexes cytochromeb 6 f and photosystem I. Here we review the combination of experimental efforts in the literature to unveil the functional and structural features of the complex between cytochrome f and plastocyanin, which have widely been used as a suitable model for analyzing transient redox interactions.