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Literature summary extracted from

  • Bogachev, A.V.; Bloch, D.A.; Bertsova, Y.V.; Verkhovsky, M.I.
    Redox properties of the prosthetic groups of Na(+)-translocating NADH:quinone oxidoreductase. 2. Study of the enzyme by optical spectroscopy (2009), Biochemistry, 48, 6299-6304.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.1.1 Fe the enzyme contains one [2Fe-2S] cluster Vibrio harveyi

Organism

EC Number Organism UniProt Comment Textmining
7.2.1.1 Vibrio harveyi
-
-
-

Synonyms

EC Number Synonyms Comment Organism
7.2.1.1 Na+-NQR
-
 Vibrio harveyi
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
 Vibrio harveyi
7.2.1.1 NADH:quinone oxidoreductase
-
 Vibrio harveyi

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.1.1 FAD the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stays in the anionic form in the fully reduced enzyme Vibrio harveyi
7.2.1.1 FMN the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stayed in the anionic form in the fully reduced enzyme Vibrio harveyi
7.2.1.1 riboflavin the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stays in the anionic form in the fully reduced enzyme Vibrio harveyi