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TitleThe Unusual Homodimer of a Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors.
Journal, issue, pagesAngew Chem Int Ed Engl, Vol. 60, Issue 24, Page 13323-13330, Year 2021
Publish dateJun 7, 2021
AuthorsGuoliang Zhu / Hui Zeng / Shuangbo Zhang / Jana Juli / Linhua Tai / Danyang Zhang / Xiaoyun Pang / Yan Zhang / Sin Man Lam / Yun Zhu / Guohong Peng / Hartmut Michel / Fei Sun /
PubMed AbstractThe heme-copper oxidase superfamily comprises cytochrome c and ubiquinol oxidases. These enzymes catalyze the transfer of electrons from different electron donors onto molecular oxygen. A B-family ...The heme-copper oxidase superfamily comprises cytochrome c and ubiquinol oxidases. These enzymes catalyze the transfer of electrons from different electron donors onto molecular oxygen. A B-family cytochrome c oxidase from the hyperthermophilic bacterium Aquifex aeolicus was discovered previously to be able to use both cytochrome c and naphthoquinol as electron donors. Its molecular mechanism as well as the evolutionary significance are yet unknown. Here we solved its 3.4 Å resolution electron cryo-microscopic structure and discovered a novel dimeric structure mediated by subunit I (CoxA2) that would be essential for naphthoquinol binding and oxidation. The unique structural features in both proton and oxygen pathways suggest an evolutionary adaptation of this oxidase to its hyperthermophilic environment. Our results add a new conceptual understanding of structural variation of cytochrome c oxidases in different species.
External linksAngew Chem Int Ed Engl / PubMed:33665933 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

30657

7deg

EMDB-30657, PDB-7deg:
Cryo-EM structure of a heme-copper terminal oxidase dimer provides insights into its catalytic mechanism
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-HAS:
HEME-AS

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-CU:
COPPER (II) ION / Copper

ChemComp-DLX:
2-[(2~{E},6~{E},10~{Z},14~{Z},18~{Z},23~{R})-3,7,11,15,19,23,27-heptamethyloctacosa-2,6,10,14,18-pentaenyl]naphthalene-1,4-dione

ChemComp-PGV:
(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipid*YM / Phosphatidylglycerol

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

ChemComp-CUA:
DINUCLEAR COPPER ION

Source
  • Aquifex aeolicus VF5 (bacteria)
  • aquifex aeolicus (strain vf5) (bacteria)
  • aquifex aeolicus (bacteria)
KeywordsOXIDOREDUCTASE / electron cryo-microscopy / heme-copper oxidase / cytochrome c oxidase dimer / Aquifex aeolicus / naphthoquinone

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