The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I

Journal of Biological Chemistry

Volumn 285, Issue 50, 2010, Pages 39070-39078

  Nakamaru Ogiso, Eiko ^a   Kao, Mou Chieh ^a,b,c   Chen, Han ^a,d   Sinha, Subhash C ^b   Yagi, Takao ^b   Ohnishi, Tomoko ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^d THIRD MILITARY MEDICAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMILORIDE; ANTIPORTERS; COMPLEX I; CONSERVED RESIDUES; CONTROL LEVEL; DIRECT COUPLING; ELECTRON TRANSFER; INDIRECT COUPLINGS; OXIDASE ACTIVITY; POINT MUTATIONS; PROTON PUMPING MECHANISM; PROTON-PUMPING; PUMPING EFFICIENCY; REDUCTASE ACTIVITY; SEQUENCE SIMILARITY; SPECIFIC INHIBITORS; TRANSMEMBRANES; WILD TYPES;

ESCHERICHIA COLI; PROTONS; SODIUM; STOICHIOMETRY;

PUMPS;

MEMBRANE PROTEIN; MEMBRANE SUBUNIT NUOL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GROWTH; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; GENE SEQUENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON TRANSPORT; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; STOICHIOMETRY; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANTIPORTERS; ELECTRONS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FURANS; GENE EXPRESSION REGULATION, BACTERIAL; GENETIC TECHNIQUES; INHIBITORY CONCENTRATION 50; MITOCHONDRIA; MOLECULAR SEQUENCE DATA; MUTATION; NADH DEHYDROGENASE; PROTON PUMPS; PROTONS; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI;

EID: 78649496491     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.157826     Document Type: Article

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