An enzymatically active artificial redox coenzyme based on a synthetic dye template

Enzyme and Microbial Technology

Volumn 20, Issue 1, 1997, Pages 2-11

  McLoughlin, Sheila B ^a,b   Lowe, Christopher R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b AgrEvo UK Limited   (United Kingdom)

Author keywords

Anthraquinone linked triazine; Artificial coenzyme; Coenzyme analogue; Oxidoreductases; Steady slate kinetics

Indexed keywords

CATALYSIS; CATALYST ACTIVITY; CHEMICAL MODIFICATION; CONFORMATIONS; DYES; ETHANOL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION; REACTION KINETICS; REDOX REACTIONS;

ANTHRAQUINONE CHROMOPHORE; ARTIFICIAL COENZYMES; HORSE LIVER ALCOHOL DEHYDROGENASE (HLADH); MICHAELIS CONSTANT; PRIMARY ALIPHATIC; STEADY STATE KINETICS; SYNTHETIC DYE TEMPLATE;

COENZYMES;

ALCOHOL DEHYDROGENASE; ALCOHOL DERIVATIVE; ANTHRAQUINONE; CIBACRON BLUE F3GA; DYE; IDITOL DEHYDROGENASE; LIVER ENZYME; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PENTANOL;

ABSORPTION SPECTROPHOTOMETRY; ARTICLE; COENZYME; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SPECIFICITY; NONHUMAN; OXIDATION REDUCTION REACTION; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 0031024466     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00074-9     Document Type: Article

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