Ontology highlight
ABSTRACT:
SUBMITTER: Sinha PK
PROVIDER: S-EPMC2665103 | biostudies-other | 2009 Apr
REPOSITORIES: biostudies-other
Sinha Prem Kumar PK Torres-Bacete Jesus J Nakamaru-Ogiso Eiko E Castro-Guerrero Norma N Matsuno-Yagi Akemi A Yagi Takao T
The Journal of biological chemistry 20090203 15
The bacterial proton-translocating NADH:quinone oxidoreductase (NDH-1) consists of two domains, a peripheral arm and a membrane arm. NuoH is a counterpart of ND1, which is one of seven mitochondrially encoded hydrophobic subunits, and is considered to be involved in quinone/inhibitor binding. Sequence comparison in a wide range of species showed that NuoH is comprehensively conserved, particularly with charged residues in the cytoplasmic side loops. We have constructed 40 mutants of 27 conserved ...[more]