Traffic within the cytochrome b6f lipoprotein complex: gating of the quinone portal.

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TitleTraffic within the cytochrome b6f lipoprotein complex: gating of the quinone portal.
Publication TypeJournal Article
Year of Publication2014
AuthorsS Hasan, S, Proctor, EA, Yamashita, E, Dokholyan, NV, Cramer, WA
JournalBiophys J
Volume107
Issue7
Pagination1620-8
Date Published2014 Oct 07
ISSN1542-0086
KeywordsBiological Transport, Cyanobacteria, Cytochrome b6f Complex, Lipoproteins, Models, Molecular, Protein Conformation, Quinones
Abstract

The cytochrome bc complexes b6f and bc1 catalyze proton-coupled quinol/quinone redox reactions to generate a transmembrane proton electrochemical gradient. Quinol oxidation on the electrochemically positive (p) interface of the complex occurs at the end of a narrow quinol/quinone entry/exit Qp portal, 11 Å long in bc complexes. Superoxide, which has multiple signaling functions, is a by-product of the p-side quinol oxidation. Although the transmembrane core and the chemistry of quinone redox reactions are conserved in bc complexes, the rate of superoxide generation is an order of magnitude greater in the b6f complex, implying that functionally significant differences in structure exist between the b6f and bc1 complexes on the p-side. A unique structure feature of the b6f p-side quinol oxidation site is the presence of a single chlorophyll-a molecule whose function is unrelated to light harvesting. This study describes a cocrystal structure of the cytochrome b6f complex with the quinol analog stigmatellin, which partitions in the Qp portal of the bc1 complex, but not effectively in b6f. It is inferred that the Qp portal is partially occluded in the b6f complex relative to bc1. Based on a discrete molecular-dynamics analysis, occlusion of the Qp portal is attributed to the presence of the chlorophyll phytyl tail, which increases the quinone residence time within the Qp portal and is inferred to be a cause of enhanced superoxide production. This study attributes a novel (to our knowledge), structure-linked function to the otherwise enigmatic chlorophyll-a in the b6f complex, which may also be relevant to intracellular redox signaling.

DOI10.1016/j.bpj.2014.08.003
Alternate JournalBiophys. J.
PubMed ID25296314
PubMed Central IDPMC4190601
Grant ListR01-GM080742 / GM / NIGMS NIH HHS / United States
R01-GM038323 / GM / NIGMS NIH HHS / United States
F31 AG039266 / AG / NIA NIH HHS / United States
F31AG039266 / AG / NIA NIH HHS / United States
R01 GM080742 / GM / NIGMS NIH HHS / United States
R01 GM038323 / GM / NIGMS NIH HHS / United States
P30 CA023168 / CA / NCI NIH HHS / United States