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TitleStructural basis for energy transduction by respiratory alternative complex III.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 1728, Year 2018
Publish dateApr 30, 2018
AuthorsJoana S Sousa / Filipa Calisto / Julian D Langer / Deryck J Mills / Patrícia N Refojo / Miguel Teixeira / Werner Kühlbrandt / Janet Vonck / Manuela M Pereira /
PubMed AbstractElectron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may ...Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.
External linksNat Commun / PubMed:29712914 / PubMed Central
MethodsEM (single particle)
Resolution3.87 Å
Structure data

EMDB-4165, PDB-6f0k:
Alternative complex III
Method: EM (single particle) / Resolution: 3.87 Å

Chemicals

ChemComp-HEC:
HEME C / Heme C

ChemComp-F3S:
FE3-S4 CLUSTER / Iron–sulfur cluster

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

Source
  • Rhodothermus marinus (bacteria)
  • Rhodothermus obamensis (bacteria)
  • rhodothermus marinus (strain atcc 43812 / dsm 4252 / r-10) (bacteria)
KeywordsMEMBRANE PROTEIN / electron transfer / quinol oxidation / respiratory chain

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