Unfolding and pH studies on manganese peroxidase: Role of heme and calcium on secondary structure stability

Biopolymers - Biospectroscopy Section

Volumn 72, Issue 1, 2003, Pages 38-47

  Banci, Lucia ^a   Bartalesi, Ilaria ^a   Ciofi Baffoni, Simone ^a   Tien, Ming ^b  

^a UNIVERSITY OF FLORENCE   (Italy)

^b NONE

Author keywords

Calcium ions; Circular dichroism; Heme; Manganese peroxidase; Protein folding

Indexed keywords

CALCIUM; ENZYMES; PEROXIDES; PH EFFECTS; PROTEINS; ULTRAVIOLET SPECTROSCOPY;

SECONDARY STRUCTURE STABILITY;

MANGANESE COMPOUNDS;

CALCIUM ION; HEME; MANGANESE PEROXIDASE;

ACIDITY; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PH MEASUREMENT; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS; ULTRAVIOLET RADIATION;

APOPROTEINS; CALCIUM; CIRCULAR DICHROISM; DITHIOTHREITOL; ENZYME STABILITY; HEME; HOLOENZYMES; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; OXIDATION-REDUCTION; PEROXIDASES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; UREA;

EID: 0037236592     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10283     Document Type: Article

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