High-pressure FTIR study of the stability of horseradish peroxidase. Effect of heme substitution, ligand binding, Ca++ removal, and reduction of the disulfide bonds

Biochemistry

Volumn 42, Issue 2, 2003, Pages 553-561

  Smeller, L ^a   Meersman, F ^b   Fidy, J ^a   Heremans, K ^b  

^a SEMMELWEIS UNIVERSITY   (Hungary)

^b UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ATMOSPHERIC PRESSURE; ENZYMES; SPECTROSCOPY; STABILIZATION; SUBSTRATES;

CONFORMATIONAL MOBILITY; STABILIZING FACTORS;

CALCIUM;

CALCIUM ION; HEME DERIVATIVE; HORSERADISH PEROXIDASE; ISOENZYME; LIGAND;

ARTICLE; CALCIUM BINDING; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ANALYSIS; ENZYME STABILITY; FOURIER ANALYSIS; LIGAND BINDING; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; REDUCTION;

AMIDES; APOENZYMES; BINDING SITES; CALCIUM; DISULFIDES; ENZYME STABILITY; HEME; HORSERADISH PEROXIDASE; HYDROXAMIC ACIDS; LIGANDS; METALS; OXIDATION-REDUCTION; PORPHYRINS; PRESSURE; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

ARMORACIA RUSTICANA;

EID: 0347926373     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026192n     Document Type: Article

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