EC Number   |
Natural Substrates |
|---|
    7.1.1.2 | more |
complex I is a primary electrogenic proton pump and may be capable of secondary sodium antiport. The magnitude of the pH-gradient depends on the sodium concentration |
| 7.1.1.2 | more |
superoxide production from complex I is large under conditions of reverse electron transport. Production of superoxide by complex I during reverse electron transport is at least 3fold more sensitive to the pH gradient than to the membrane potential |
| 7.1.1.2 | more |
superoxide production rates by complex I during reverse electron transfer are much greater than during forwards electron transfer. The major site of superoxide production in complex I is the quinpone-binding site, it is most likely a semiquinone |
| 7.1.1.2 | more |
the enzyme mediates electron transfer to particulate methane monooxygenase |
| 7.1.1.2 | more |
FMN-dependent NADH-quinone reductase induced by menadione |
| 7.1.1.2 | more |
NADH:ubiquinone oxidoreductase (EC 1.6.5.3) constitutes the entry point of electrons in the electron transport chain. Mitochondrial NADH:ubiquinone oxidoreductase or complex I (CI) is a frequently affected enzyme in cases of mitochondrial disorders |
| 7.1.1.2 | more |
no redox-coupled Na+ transport and no Na+/H+ antiporter function by the enzyme from Yarrowia lipolytica |
| 7.1.1.2 | more |
no redox-coupled Na+ transport, but the deactive form of complex I, which is formed spontaneously when enzyme turnover is precluded by lack of substrates, is a Na+/H+ antiporter. The antiporter activity is Na+-specific and is abolished upon reactivation by the addition of substrates and by the complex I inhibitor rotenone. It is specific for Na+ over K+ |
| 7.1.1.2 | NADH + H+ + menaquinone |
the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Mycobacterium tuberculosis is the causative agents of tuberculosis). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. Mycobacterium tuberculosis contains a branched respiratory chain terminating in a cytochrome bd (quinol) oxidase and an aa3-type cytochrome c oxidase. Both chains are fed by a menaquinol (MQH2) pool that is generated by four dehydrogenases; one succinate menaquinone oxidoreductase (SQR), one multimeric type I NADH: dehydrogenase (complex I), and two type II NADH: menaquinone oxidoreductases (ndh and ndhA). Transposon insertion knockout strategy reveals that disruption of the ndh gene is lethal |
| 7.1.1.2 | NADH + H+ + ubiquinone |
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