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Updated: Aug 13, 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
Cytochrome bc complexes: a common core of structure and function surrounded by diversity in the outlying provinces
Janet L Smith1, Huamin Zhang, Jiusheng Yan
1Department of Biological Sciences, 915 West State Street, Purdue University, West Lafayette, Indiana 47907-2054, USA. smithj@purdue.edu
Abstract:
The atomic-level picture of transmembrane protein complexes in the photosynthetic membrane has now been completed by the recent publication of crystal structures of cytochrome b(6)f and photosystem II. The two structures of cytochrome b(6)f, together with previously reported structures of the cytochrome bc(1) respiratory complex, provide a basis for understanding the central electron and proton transfer events of photosynthesis and respiration. The protein structures and charge transfer events within the core of the complexes are highly similar, but the complexes differ in subunit and chromophore composition in proportion to the distance from the central redox site within the membrane near the electropositive side.
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