Literature summary for 7.1.1.9 extracted from

Ishigami, I.; Zatsepin, N.A.; Hikita, M.; Conrad, C.E.; Nelson, G.; Coe, J.D.; Basu, S.; Grant, T.D.; Seaberg, M.H.; Sierra, R.G.; Hunter, M.S.; Fromme, P.; Fromme, R.; Yeh, S.R.; Rousseau, D.L.
Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature (2017), Proc. Natl. Acad. Sci. USA, 114, 8011-8016 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
room temperature, pH 6.8, damage-free structure in the carbon monoxide-bound state at a resolution of 2.3 A. In the femtosecond X-ray crystallography structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of about 142°. In the synchrotron structure, the Fe-CO bond is cleaved. CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by about 0.38 Å. Ligand binding to the heme a3 iron in the femtosecond X-ray crystallography structure is associated with an allosteric structural transition	Bos taurus

Crystallization (Comment)

Organism

room temperature, pH 6.8, damage-free structure in the carbon monoxide-bound state at a resolution of 2.3 A. In the femtosecond X-ray crystallography structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of about 142°. In the synchrotron structure, the Fe-CO bond is cleaved. CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by about 0.38 Å. Ligand binding to the heme a3 iron in the femtosecond X-ray crystallography structure is associated with an allosteric structural transition

Bos taurus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P00396	-	-

Synonyms

Synonyms	Comment	Organism
cytochrome c oxidase subunit 1	-	Bos taurus
MT-CO1	-	Bos taurus

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Release 2023.1 (January 2023)