ChemBioChem · 2002 · 43 citations · 20 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryRedox BiochemistryAntioxidant DefenseElectron Transfer In ProteinsRedox EnzymesCytochrome Electron TransferCytochrome EnzymesHeme EnzymesHeme Redox Enzyme MechanismsPeroxidase EnzymesPeroxidase InactivationProtein Matrix OrganizationProtein-matrix Interactions
Unraveling enzyme activity: Unfolding of the electron-transfer protein cytochrome c-550 results in a spectacular increase in its peroxidase activity (see graph). This finding is interpreted in terms of the suppression by the cytochrome protein matrix of the potentially harmful peroxidase activity inherent to its heme cofactor.
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Protein Folding Intermediates: Native-State Hydrogen Exchange
Yawen Bai, Tobin R. Sosnick, Leland Mayne et al. · Science · 1995 · 999 citations
Fundamentals of enzyme kinetics
Choice Reviews Online · 1996 · 664 citations
Cytochromes c: evolutionary structural and physicochemical aspects
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Life Sciences, Biochemistry, Biology +11