Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41 Val, with altered reactivity towards hydrogen peroxide and reducing substrates
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1992.tb17077.x/fullpdf
Reference51 articles.
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2. On the function and mechanism of action of peroxidases
3. Structural characterization of horseradish peroxidase using EXAFS spectroscopy. Evidence for Fe = O ligation in compounds I and II
4. Identification by ENDOR of Trp 191 as the Free-Radical Site in Cytochrome c Peroxidase Compound ES
5. Recent ENDOR and Pulsed Electron Paramagnetic Resonance Studies of CytochromecPeroxidase - Compound I and Its Site-Directed Mutants
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