6NMP

SFX structure of oxidized cytochrome c oxidase at room temperature

Summary for 6NMP

• Entry DOI: 10.2210/pdb6nmp/pdb
• Related: 6NKN 6NMF
• Descriptor: Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 7A1, mitochondrial, Cytochrome c oxidase subunit 7B, mitochondrial, ... (28 entities in total)
• Functional Keywords: complex iv, membrane protein, terminal enzyme, electron transfer, oxidoreductase
• Biological source: Bos taurus (Bovine); More
• Total number of polymer chains: 26
• Total formula weight: 442820.00

Authors

Rousseau, D.L.,Yeh, S.-R.,Ishigami, I. (deposition date: 2019-01-11, release date: 2019-03-13, Last modification date: 2023-10-11)

Primary citation

Ishigami, I.,Lewis-Ballester, A.,Echelmeier, A.,Brehm, G.,Zatsepin, N.A.,Grant, T.D.,Coe, J.D.,Lisova, S.,Nelson, G.,Zhang, S.,Dobson, Z.F.,Boutet, S.,Sierra, R.G.,Batyuk, A.,Fromme, P.,Fromme, R.,Spence, J.C.H.,Ros, A.,Yeh, S.R.,Rousseau, D.L.
Snapshot of an oxygen intermediate in the catalytic reaction of cytochromecoxidase.
Proc. Natl. Acad. Sci. U.S.A., 116:3572-3577, 2019

PubMed Abstract: Cytochrome oxidase (CO) reduces dioxygen to water and harnesses the chemical energy to drive proton translocation across the inner mitochondrial membrane by an unresolved mechanism. By using time-resolved serial femtosecond crystallography, we identified a key oxygen intermediate of bovine CO. It is assigned to the P-intermediate, which is characterized by specific redox states of the metal centers and a distinct protein conformation. The heme iron atom is in a ferryl (Fe = O) configuration, and heme and Cu are oxidized while Cu is reduced. A Helix-X segment is poised in an open conformational state; the heme farnesyl sidechain is H-bonded to S382, and loop-I-II adopts a distinct structure. These data offer insights into the mechanism by which the oxygen chemistry is coupled to unidirectional proton translocation.

PubMed: 30808749
DOI: 10.1073/pnas.1814526116

Experimental method

X-RAY DIFFRACTION (2.9 Å)