Subunit composition of NADH dehydrogenase (quinone) = [subunit of NADH dehydrogenase (quinone)]2
This NADH dehydrogenase enzyme is thought to compete with the one-electron reduction pathway of quinones, which is potentially toxic as it generates superoxide radicals and hydrogen peroxide [Hayashi90].
The intracellular level of this enzyme is increased 23-fold by growth in the presence of 0.3 mM menadione, but not paraquat [Hayashi90]. The critical inductive signal is a 2-alkyl-1.4-quinone structure with an unsubstitued or Br-substituted C-3 [Unemoto92].
Molecular Weight of Polypeptide: 24.0 kD (experimental) [Hayashi90 ]
Molecular Weight of Multimer: 50 kD (experimental) [Hayashi90]
Instance reaction of [a quinone + NAD(P)H + H+ → a quinol + NAD(P)+] (220.127.116.11):
|Cellular Component:||GO:0005829 - cytosol [Hayashi90]|
Enzymatic reaction of: NADH dehydrogenase (quinone)
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Reversibility of this reaction is unspecified.
pH(opt): 7-8 [Hayashi90]
Hayashi90: Hayashi M, Hasegawa K, Oguni Y, Unemoto T (1990). "Characterization of FMN-dependent NADH-quinone reductase induced by menadione in Escherichia coli." Biochim Biophys Acta 1990;1035(2);230-6. PMID: 2118386
Unemoto92: Unemoto T, Shimada H, Hayashi M (1992). "Chemical structures critical for the induction of FMN-dependent NADH-quinone reductase in Escherichia coli." Biochim Biophys Acta 1099(2);170-4. PMID: 1543701
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493