[Structure and biogenesis of cytochrome b6f complex]
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Updated: Jun 18, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Katarzyna A Hombek-Urban1, Jarosław Króliczewski, Andrzej Szczepaniak
1Department of Hygiene, Wroclaw Medical University, 7 Mikulicza-Radeckiego St., 50-345 Wroclaw, Poland. kasiahombekurban@hyg.am.wroc.pl
Abstract:
Both photosynthetic cytochrome b6f complex, and respiratory cytochrome bc1 belong to the family of cytochrome bc complexes. Both protein supercomplexes participate in the transport of electrons, proton translocation through the biological membrane, and they catalyze chinon oxidation as well. The function, composition, spatial organization and biosynthesis of cytochrome b6f complex has been being the subject of research for years. The obtained crystal structures revealed the presence of the third haem in the cytochrome b6, whereas mutagenic experiments indicated the participation of the additional protein factor (TCA) engaged in the regulation of b6f cytochrome complex synthesis through the interaction between TCA and 5'UTR of the PETA transcript. The following compendium is the collection of the current data and knowledge with reference to the structure and biogenesis of the above mentioned protein complex.
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