Functional implications from an unexpected position of the 49-kDa subunit of NADH:Ubiquinone oxidoreductase

Journal of Biological Chemistry

Volumn 278, Issue 31, 2003, Pages 29072-29078

  Zickermann, Volker ^a   Bostina, Mihnea ^b   Hunte, Carola ^b   Ruiz, Teresa ^b,c   Radermacher, Michael ^b,c   Brandt, Ulrich ^a  

^a GOETHE UNIVERSITY   (Germany)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^c UNIVERSITY OF VERMONT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELL MEMBRANES; COMPLEXATION; CONFORMATIONS; ENERGY TRANSFER; PATHOLOGY; PROTONS; REDUCTION;

PROTON TRANSLOCATION;

ENZYME KINETICS;

PROTON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

ARTICLE; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ENERGY TRANSFER; ENZYME ACTIVITY; ENZYME SUBUNIT; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON TRANSPORT; REDUCTION; RESPIRATORY CHAIN;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; ANTIBODY SPECIFICITY; BINDING SITES; ELECTRON TRANSPORT COMPLEX I; ENERGY TRANSFER; EPITOPE MAPPING; FEMALE; MICE; MICE, INBRED BALB C; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; NADH, NADPH OXIDOREDUCTASES; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PROTON PUMPS; SEQUENCE HOMOLOGY; YARROWIA;

EID: 0043208847     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M302713200     Document Type: Article

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