An EPR, thermostability and pH-dependence study of wild-type and mutant forms of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13

BioMetals

Volumn 26, Issue 1, 2013, Pages 75-84

  Caglio, Raffaella ^a   Pessione, Enrica ^a   Valetti, Francesca ^a   Giunta, Carlo ^a   Ghibaudi, Elena ^a  

^a UNIVERSITY OF TURIN   (Italy)

Author keywords

Aromatic compound degradation; EPR spectroscopy; Intradiol dioxygenase; Iron containing enzyme; Protein stability; Structure function relationships

Indexed keywords

CATECHOL 1,2 DIOXYGENASE; DISSOLVED OXYGEN;

ACINETOBACTER; ACINETOBACTER RADIORESISTENS; ARTICLE; BIOTECHNOLOGY; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; IRON BINDING CAPACITY; MUTANT; NONHUMAN; OXYGEN AFFINITY; PH; SENSITIVITY ANALYSIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; TEMPERATURE SENSITIVITY; ULTRAVIOLET SPECTROSCOPY; WILD TYPE;

ACINETOBACTER; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CATECHOL 1,2-DIOXYGENASE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; OXYGEN; SOLUTIONS; TRANSITION TEMPERATURE;

ACINETOBACTER RADIORESISTENS; BACTERIA (MICROORGANISMS);

EID: 84873409868     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-012-9595-x     Document Type: Article

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