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Literature summary for 7.1.1.2 extracted from

  • Steimle, S.; Bajzath, C.; Doerner, K.; Schulte, M.; Bothe, V.; Friedrich, T.
    Role of subunit NuoL for proton translocation by respiratory complex I (2011), Biochemistry, 50, 3386-3393.
    View publication on PubMed
Search for more literature for 7.1.1.2

Protein Variants

Protein Variants Comment Organism
additional information construction of NuoL variants Y544Stop and W592Stop, that contain a stop codon leading to truncations in themiddle and at the end of the horizontal helix. The W592Stop variant is missing the C-terminal TM helix and the Y544Stop variant is missing this helix and approximately half of the amphipathic helix. Proton translocation by the mutant W592Stop variant and the Y544Stop variant after reconstitution in proteoliposomes, overview Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + ubiquinone + 6 H+[side 1] Escherichia coli
-
 NAD+ + ubiquinol + 7 H+[side 2]
-
 ?
NADH + ubiquinone + 6 H+[side 1] Escherichia coli BW25113
-
 NAD+ + ubiquinol + 7 H+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 mutant derivative of strain BW25113 from which the nuo operon is deleted by genomic replacement
-
Escherichia coli BW25113
-
 mutant derivative of strain BW25113 from which the nuo operon is deleted by genomic replacement
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + ubiquinone + 6 H+[side 1]
-
 Escherichia coli NAD+ + ubiquinol + 7 H+[side 2]
-
 ?
NADH + ubiquinone + 6 H+[side 1]
-
 Escherichia coli BW25113 NAD+ + ubiquinol + 7 H+[side 2]
-
 ?

Synonyms

Synonyms Comment Organism
NADH:ubiquinone oxidoreductase
-
 Escherichia coli
respiratory complex I
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Escherichia coli

General Information

General Information Comment Organism
malfunction electron transfer and proton translocation activity of complex I variants lacking either NuoL or parts of the C-terminal domain, overview Escherichia coli
additional information the complex consists of a peripheral arm catalyzing the electron transfer reaction and a membrane arm involved in proton translocation. The energy released by the redox reaction is transmitted to the membrane arm via a conformational change in the horizontal helix. The helix corresponds to the C-terminal part of the most distal subunit NuoL. The C-terminal domain of NuoL is essential for the translocation of 2H+/2e- Escherichia coli
physiological function respiratory complex I couples the transfer of electrons from NADH to ubiquinone with a translocation of protons across the membrane Escherichia coli