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Volumn 6, Issue 4, 2005, Pages 747-758

The effects of ligand exchange and mobility on the peroxidase activity of a bacterial cytochrome c upon unfolding

(7) Worrall, Jonathan A R a Diederix, Rutger E M a Prudêncio, Miguel a Lowe, Christian E a,b Ciofi Baffoni, Simone b Ubbink, Marcellus a Canters, Gerard W a

a LEIDEN UNIVERSITY (Netherlands)

b UNIVERSITY OF FLORENCE (Italy)

Author keywords

Heme proteins; Metalloenzymes; NMR spectroscopy; Peroxidases; Protein unfolding

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME C; GLUTAMIC ACID; GLUTAMINE; HEME; HISTIDINE; LYSINE; MITOCHONDRIAL ENZYME; MUTANT PROTEIN; PEROXIDASE;

ARTICLE; CONCENTRATION (PARAMETERS); ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; ION EXCHANGE CHROMATOGRAPHY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARACOCCUS VERSUTUS; PH; PRIORITY JOURNAL; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; WILD TYPE;

AMINO ACID SUBSTITUTION; CYTOCHROME C GROUP; GUANIDINE; HEME; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; PARACOCCUS; PEROXIDASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROPHOTOMETRY; SPECTROPHOTOMETRY, ULTRAVIOLET; THERMODYNAMICS;

PARACOCCUS VERSUTUS;

EID: 18944387200 PISSN: 14394227 EISSN: None Source Type: Journal
DOI: 10.1002/cbic.200400291 Document Type: Article

Times cited : (5)

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