Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus

European Journal of Biochemistry

Volumn 270, Issue 24, 2003, Pages 4887-4897

  Žoldák, Gabriel ^a   Šut'ák, Róbert ^a,b   Antalík, Marián ^a,c   Sprinzl, Mathias ^d   Sedlák, Erik ^a  

^a P J AFÁRIK UNIVERSITY   (Slovakia)

^b CHARLES UNIVERSITY   (Czech Republic)

^c INSTITUTE OF EXPERIMENTAL PHYSICS   (Slovakia)

^d UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Conformational dynamics; Flavoproteins; Fluorescence quenching; NADH oxidase; Thermus thermophilus

Indexed keywords

FLAVOPROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UREA;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; STEADY STATE; TEMPERATURE; THERMUS THERMOPHILUS;

BINDING SITES; CATALYSIS; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FLAVINS; KINETICS; MODELS, MOLECULAR; MULTIENZYME COMPLEXES; NADH, NADPH OXIDOREDUCTASES; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS; THERMUS THERMOPHILUS; TIME FACTORS; TRYPTOPHAN; UREA;

THERMUS; THERMUS THERMOPHILUS;

EID: 17444434923     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03889.x     Document Type: Article

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