Disruption of the H-bond network in the main access channel of catalase-peroxidase modulates enthalpy and entropy of Fe(III) reduction

Journal of Inorganic Biochemistry

Volumn 104, Issue 6, 2010, Pages 648-656

  Vlasits, Jutta ^a   Bellei, Marzia ^b   Jakopitsch, Christa ^a   De Rienzo, Francesca ^b,c   Furtmüller, Paul G ^a   Zamocky, Marcel ^a   Sola, Marco ^b,c   Battistuzzi, Gianantonio ^b   Obinger, Christian ^a  

^a UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

^b UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

^c CNR   (Italy)

Author keywords

Catalase activity; Catalase peroxidase; Enthalpy; Entropy; Redox thermodynamics; Reduction potential

Indexed keywords

ARGININE; CATALASE; FERRIC ION; FERROUS ION; HEME; HISTIDINE; HYDROGEN PEROXIDE; KATG PROTEIN; METHIONINE; MUTANT PROTEIN; PEROXIDASE; SOLVENT; TRYPTOPHAN; TYROSINE;

ARTICLE; CATALYSIS; CHEMICAL MODIFICATION; ENTHALPY; ENTROPY; HYDROGEN BOND; OXIDATION REDUCTION REACTION; STATIC ELECTRICITY; SYNECHOCYSTIS; TEMPERATURE SENSITIVITY; WILD TYPE;

CATALASE; ENDOPEPTIDASES; ENTROPY; FERRIC COMPOUNDS; MODELS, MOLECULAR; OXIDATION-REDUCTION; PEROXIDASES; SYNECHOCYSTIS; THERMODYNAMICS;

SYNECHOCYSTIS;

EID: 77952546410     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2010.02.006     Document Type: Article

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