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Literature summary for 7.1.1.2 extracted from

  • Larosa, V.; Coosemans, N.; Motte, P.; Bonnefoy, N.; Remacle, C.
    Reconstruction of a human mitochondrial complex I mutation in the unicellular green alga Chlamydomonas (2012), Plant J., 70, 759-768.
    View publication on PubMed
Search for more literature for 7.1.1.2

Protein Variants

Protein Variants Comment Organism
L158P site-directed mutagenesis, introducetion of a Leu157Pro substitution into the Chlamydomonas ND4 subunit of complex I in two recipient strains by biolistic transformation Chlamydomonas sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Chlamydomonas sp.
-
-
-
Homo sapiens
-
-
-

Synonyms

Synonyms Comment Organism
complex I
-
 Homo sapiens
complex I
-
 Chlamydomonas sp.
NADH:ubiquinone oxidoreductase
-
 Homo sapiens
NADH:ubiquinone oxidoreductase
-
 Chlamydomonas sp.

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction defects in complex I are the most frequent cause of human respiratory disorders. Substitution L158P does not lead to any respiratory enzyme defects when present in the heteroplasmic state in a patient with chronic progressive external ophthalmoplegia Homo sapiens
malfunction when present in the homoplasmic state in the alga, the mutation does not prevent assembly of the whole complex I, the NADH dehydrogenase activity of the peripheral arm of the complex is mildly affected. The NADH:duroquinone oxidoreductase activity is strongly reduced, suggesting that the substitution could affect binding of ubiquinone to the membrane domain. The membrane potential is not affected in mutant mitochondria. The in vitro defects correlate with a decrease in dark respiration and growth rate in vivo, phenotype, overview Chlamydomonas sp.