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Literature summary for 7.1.1.2 extracted from

  • Sharpley, M.S.; Hirst, J.
    The inhibition of mitochondrial complex I (NADH:ubiquinone oxidoreductase) by Zn2+ (2006), J. Biol. Chem., 281, 34803-34809.
    View publication on PubMed
Search for more literature for 7.1.1.2

Inhibitors

Inhibitors Comment Organism Structure
Ba2+ 1 mM Bos taurus
Ca2+ 1 mM Bos taurus
Cd2+ 1 mM, potent inhibitor Bos taurus
Co2+ 1 mM Bos taurus
Cu2+ 1 mM Bos taurus
Mn2+ 1 mM Bos taurus
Ni2+ 1 mM, potent inhibitor Bos taurus
Zn2+ pH-dependent potent inhibitor, IC50: 0.01-0.05 mM at pH 7.5, depending on the enzyme state, Zn2+ does not inhibit NADH oxidation or intramolecular electron transfer, so it probably inhibits either proton transfer to bound quinone or proton translocation. Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial membrane
-
 Bos taurus 31966
-

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + decylubiquinone
-
 Bos taurus NAD+ + decylubiquinol
-
 ?
NADH + hexaamineruthenium(III) chloride
-
 Bos taurus NAD+ + ?
-
 ?

Synonyms

Synonyms Comment Organism
complex I
-
 Bos taurus
NADH:ubiquinone oxidoreductase
-
 Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Bos taurus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.01 0.05 pH-dependent potent inhibitor, IC50: 0.01-0.05 mM at pH 7.5, depending on the enzyme state, Zn2+ does not inhibit NADH oxidation or intramolecular electron transfer, so it probably inhibits either proton transfer to bound quinone or proton translocation. Bos taurus Zn2+