Cryo-EM structure of a heme-copper terminal oxidase dimer provides insights into its catalytic mechanism
收藏Protein Data Bank Japan2025-09-17 更新2026-03-21 收录
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Cryo-EM structure of a heme-copper terminal oxidase dimer provides insights into its catalytic mechanism Descriptor: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE, 1,2-Distearoyl-sn-glycerophosphoethanolamine, 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, ... Authors: Fei, S, Hartmut, M, Yun, Z, Guoliang, Z, Shuangbo, Z. Deposit date: 2020-11-04 Release date: 2021-08-04 Last modified: 2025-09-17 Method: ELECTRON MICROSCOPY (3.4 Å) Cite: The Unusual Homodimer of a Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors. Angew.Chem.Int.Ed.Engl., 60, 2021
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2020-11-04
