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Literature summary for 7.1.1.9 extracted from

  • Liang, R.; Swanson, J.M.J.; Wikstroem, M.; Voth, G.A.
    Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase (2017), Proc. Natl. Acad. Sci. USA, 114, 5924-5929 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
N139C in this mutants, proton back leakage through the D-channel is kinetically favored over proton pumping due to the loss of a kinetic gate in the N139 region Cereibacter sphaeroides
N139L in this mutant, the bulky L139 side chain inhibits timely reprotonation of E286 through the D-channel, which impairs both proton pumping and the chemical reaction Cereibacter sphaeroides
N139T in this mutants, proton back leakage through the D-channel is kinetically favored over proton pumping due to the loss of a kinetic gate in the N139 region Cereibacter sphaeroides
S200V/S201V in the double mutant, the proton affinity of E286 is increased, which slows down both proton pumping and the chemical catalysis Cereibacter sphaeroides

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ contains copper Cereibacter sphaeroides
Fe3+ contains iron Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ferrocytochrome c + O2 + H+ Cereibacter sphaeroides
-
ferricytochrome c + H2O
-
?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides P33517
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + O2 + H+
-
Cereibacter sphaeroides ferricytochrome c + H2O
-
?

Synonyms

Synonyms Comment Organism
CCO
-
Cereibacter sphaeroides
cytochrome c oxidase
-
Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
heme
-
Cereibacter sphaeroides