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Literature summary for 7.1.1.9 extracted from

  • Shinzawa-Itoh, K.; Sugimura, T.; Misaki, T.; Tadehara, Y.; Yamamoto, S.; Hanada, M.; Yano, N.; Nakagawa, T.; Uene, S.; Yamada, T.; Aoyama, H.; Yamashita, E.; Tsukihara, T.; Yoshikawa, S.; Muramoto, K.
    Monomeric structure of an active form of bovine cytochrome c oxidase (2019), Proc. Natl. Acad. Sci. USA, 116, 19945-19951 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
oxidized and reduced structures of monomer with resolutions of 1.85 and 1.95 A, respectively. A hydrogen bond network of water molecules is formed at the entry surface of the proton transfer pathway, in monomeric CcO, whereas this network is altered in dimeric CcO. Phospholipid structures are found with the protein complex, two cardiolipins are found at the interface region of the supercomplex Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Bos taurus 16020
-
mitochondrion
-
Bos taurus 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
210000
-
gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00396 subunit 1
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-

Subunits

Subunits Comment Organism
monomer 1 210000, calculated from sequence Bos taurus
More dilution of the purified protein causes dissociation of the dimer to the monomer. When the pH is raised to 7.4 or 8.5, the protein also shifts from the dimer to the monomer. In solution, CcO is in an equilibrium state between the dimer and monomer Bos taurus

Synonyms

Synonyms Comment Organism
CCO
-
Bos taurus
MT-CO1
-
Bos taurus