Mutagenesis of the L, M, and N subunits of complex I from escherichia coli indicates a common role in function

PLoS ONE

Volumn 6, Issue 2, 2011, Pages

  Michel, Jose ^a   DeLeon Rangel, Jessica ^a   Zhu, Shaotong ^a   van Ree, Kalie ^a   Vik, Steven B ^a  

^a SOUTHERN METHODIST UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTER; CAPSAICIN; DECYLUBIQUINONE; GLUTAMIC ACID; LYSINE; MUTANT PROTEIN; PROTEIN SUBUNIT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINONE DERIVATIVE; UNCLASSIFIED DRUG; MULTIPROTEIN COMPLEX;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL STRAIN; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INHIBITION; ESCHERICHIA COLI; LOSS OF FUNCTION MUTATION; MEMBRANE VESICLE; NONHUMAN; OPERON; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; WILD TYPE; AMINO ACID SEQUENCE; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; TRANSGENIC ORGANISM;

ESCHERICHIA COLI;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ELECTRON TRANSPORT COMPLEX I; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; LYSINE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; MUTAGENESIS, SITE-DIRECTED; ORGANISMS, GENETICALLY MODIFIED; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS;

EID: 79952236392     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017420     Document Type: Article

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