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Literature summary for 7.1.1.4 extracted from

  • Gilderson, G.; Aagaard, A.; Gomes, C.M.; Adelroth, P.; Teixeira, M.; Brzezinski, P.
    Kinetics of electron and proton transfer during O(2) reduction in cytochrome aa(3) from A. ambivalens: an enzyme lacking Glu(I-286) (2001), Biochim. Biophys. Acta, 1503, 261-270.
    View publication on PubMed
Search for more literature for 7.1.1.4

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Acidianus ambivalens 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
caldariellaquinol + O2 + n H+/in Acidianus ambivalens
-
 caldariellaquinone + H2O + n H+/out
-
 ?
caldariellaquinol + O2 + n H+/in Acidianus ambivalens DSM 3772
-
 caldariellaquinone + H2O + n H+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Acidianus ambivalens
-
-
-
Acidianus ambivalens DSM 3772
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Acidianus ambivalens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
caldariellaquinol + O2 + n H+/in
-
 Acidianus ambivalens caldariellaquinone + H2O + n H+/out
-
 ?
caldariellaquinol + O2 + n H+/in two kinetic phases are observed. The first phase is attributed to binding of O2 to heme a3 and oxidation of both hemes forming the peroxy intermediate. The second phase is associated with proton uptake from solution and it is attributed to formation of the oxo-ferryl state, the final state in the absence of quinol. In the presence of bound caldariella quinol, heme a is re-reduced by caldariella quinol with a rate of 670/s, followed by transfer of the fourth electron to the binuclear center with a rate of 50/s. Thus the quinol donates electrons to heme a, followed by intramolecular transfer to the binuclear center Acidianus ambivalens caldariellaquinone + H2O + n H+/out
-
 ?
caldariellaquinol + O2 + n H+/in
-
 Acidianus ambivalens DSM 3772 caldariellaquinone + H2O + n H+/out
-
 ?
caldariellaquinol + O2 + n H+/in two kinetic phases are observed. The first phase is attributed to binding of O2 to heme a3 and oxidation of both hemes forming the peroxy intermediate. The second phase is associated with proton uptake from solution and it is attributed to formation of the oxo-ferryl state, the final state in the absence of quinol. In the presence of bound caldariella quinol, heme a is re-reduced by caldariella quinol with a rate of 670/s, followed by transfer of the fourth electron to the binuclear center with a rate of 50/s. Thus the quinol donates electrons to heme a, followed by intramolecular transfer to the binuclear center Acidianus ambivalens DSM 3772 caldariellaquinone + H2O + n H+/out
-
 ?

Synonyms

Synonyms Comment Organism
cytochrome aa3
-
 Acidianus ambivalens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information two kinetic phases are observed. The first phase is attributed to binding of O2 to heme a3 and oxidation of both hemes forming the peroxy intermediate. The second phase is associated with proton uptake from solution and it is attributed to formation of the oxo-ferryl state, the final state in the absence of quinol. In the presence of bound caldariella quinol, heme a is re-reduced by caldariella quinol with a rate of 670/s, followed by transfer of the fourth electron to the binuclear center with a rate of 50/s Acidianus ambivalens