A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1993.tb17654.x/fullpdf
Reference36 articles.
1. Structure of Horseradish Perosidase Compound I. Kinetic Evidence for the Incorporation of One Oxygen Atom from the Oxidizing Substrate into the Enzyme
2. Isolation and Properties of Basic Isoenzymes of Horseradish Peroxidase1
3. Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase.
4. Elementary steps in the formation of horseradish peroxidase compound I: direct observation of compound 0, a new intermediate with a hyperporphyrin spectrum
5. Elementary steps in the reaction of horseradish peroxidase with several peroxides: kinetics and thermodynamics of formation of compound 0 and compound I
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