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Volumn 77, Issue 3-4, 1999, Pages 185-195
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Thermolysis of coenzymes B12 at physiological temperatures: Activation parameters for cobalt-carbon bond homolysis and a quantitative analysis of the perturbation of the homolysis equilibrium by the ribonucleoside triphosphate reductase from Lactobacillus leichmannii
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Author keywords
Coenzyme B12; Ribonucleoside triphosphate reductase; Thermolysis
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Indexed keywords
CARBON;
COBALT;
COBAMAMIDE;
OXIDOREDUCTASE;
PHOSPHATE;
RIBONUCLEOSIDE DERIVATIVE;
RIBONUCLEOSIDE TRIPHOSPHATE REDUCTASE;
RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE;
RIBONUCLEOTIDE REDUCTASE;
ARTICLE;
BINDING KINETICS;
CHEMICAL BINDING;
ENTHALPY;
ENTROPY;
ENZYME ACTIVE SITE;
ENZYME DEGRADATION;
EQUILIBRIUM CONSTANT;
LACTOBACILLUS;
NONHUMAN;
TEMPERATURE DEPENDENCE;
BINDING SITE;
CHEMICAL MODEL;
ENZYMOLOGY;
HEAT;
HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;
KINETICS;
METABOLISM;
ULTRAVIOLET SPECTROPHOTOMETRY;
BINDING SITES;
CARBON;
CHROMATOGRAPHY, HIGH PRESSURE LIQUID;
COBALT;
COBAMIDES;
HEAT;
KINETICS;
LACTOBACILLUS;
MODELS, CHEMICAL;
RIBONUCLEOTIDE REDUCTASES;
SPECTROPHOTOMETRY, ULTRAVIOLET;
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EID: 0033233235
PISSN: 01620134
EISSN: None
Source Type: Journal
DOI: 10.1016/S0162-0134(99)00190-7 Document Type: Article |
Times cited : (44)
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References (98)
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