Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Li+ | in presence of Li+, transmembrane voltage is generally lower than in presence of Na+, and the pH profile of electron transfer activity does not reveal a pronounced maximum | Vibrio cholerae serotype O1 | |
Na+ | in presence of Na+, transmembrane voltage is barely influenced by pH (6.5-8.5), while quinone reduction activity exhibits a maximum at pH 7.5-8.0 | Vibrio cholerae serotype O1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio cholerae serotype O1 | Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 | Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon. | - |
Vibrio cholerae serotype O1 ATCC 39315 | Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 | Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon. | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the coupling efficiency of NQR is influenced by the nature of the transported cation, and by the concentration of protons. Partial uncoupling of the NQR observed with Li+, or with Na+ at pH 7.5-8.0, may be caused by the backflow of the coupling cation through the channel in subunit NqrB | Vibrio cholerae serotype O1 | ? | - |
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additional information | the coupling efficiency of NQR is influenced by the nature of the transported cation, and by the concentration of protons. Partial uncoupling of the NQR observed with Li+, or with Na+ at pH 7.5-8.0, may be caused by the backflow of the coupling cation through the channel in subunit NqrB | Vibrio cholerae serotype O1 ATCC 39315 | ? | - |
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