Activity, stability, and unfolding of reconstituted horseradish peroxidase with modified heme

Journal of Molecular Catalysis B: Enzymatic

Volumn 57, Issue 1-4, 2009, Pages 48-54

  Song, Hai Yan ^a,b   Liu, Jian Zhong ^a   Weng, Li Ping ^a   Ji, Liang Nian ^a  

^a SUN YAT SEN UNIVERSITY   (China)

^b SOUTH CHINA NORMAL UNIVERSITY   (China)

Author keywords

Catalytic properties; Chemical modification of heme; Horseradish peroxidase; Reconstitution; Stability

Indexed keywords

ACTIVE SITE; AQUEOUS BUFFER; AROMATIC MOIETIES; CATALYTIC EFFICIENCIES; CATALYTIC PROPERTIES; CONTROL ACTIVITIES; ELECTRONWITHDRAWING; ENTROPY CHANGES; HELIX CONTENT; HORSERADISH PEROXIDASE; INITIAL RATE; P-NITROPHENOL; RECONSTITUTION; SUBSTRATE-BINDING; THERMAL DENATURATIONS;

AMINO ACIDS; CHEMICAL MODIFICATION; CHEMICAL STABILITY; CONFORMATIONS; ELECTRON AFFINITY; ELECTRONS; HYDROPHOBICITY; PHENOLS; PORPHYRINS; PYROLYSIS; STABILITY; SUBSTRATES;

HEMOGLOBIN;

4 NITROPHENOL; BUFFER; HEME; HEME DERIVATIVE; HORSERADISH PEROXIDASE; N,N DIMETHYLFORMAMIDE; PARA CRESOL; PHENOL; PHENOL DERIVATIVE; SOLVENT; TRYPTOPHAN;

ALPHA HELIX; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ELECTRON; ENTHALPY; ENTROPY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME RECONSTITUTION; ENZYME STABILITY; HYDROPHOBICITY; PROTEIN DENATURATION; PROTEIN FOLDING; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

ARMORACIA RUSTICANA;

EID: 68649115119     PISSN: 13811177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcatb.2008.06.015     Document Type: Article

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