The Nature of the Intermediates in the Reactions of Fe(III)- and Mn(III)-Microperoxidase-8 with H2O2: a Rapid Kinetics Study-Reference-Cited by-同舟云学术

The Nature of the Intermediates in the Reactions of Fe(III)- and Mn(III)-Microperoxidase-8 with H2O2: a Rapid Kinetics Study

Published:2002-01-24 Issue:7 Volume:124 Page:1214-1221
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Primus Jean-Louis¹,Grunenwald Sylvie¹,Hagedoorn Peter-Leon¹,Albrecht-Gary Anne-Marie¹,Mandon Dominique¹,Veeger Cees¹

Affiliation:

1. Contribution from the Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands, Laboratoire de Physico-Chimie Bioinorganique, UMR 7509, Université Louis Pasteur, 1, rue Blaise Pascal, 67000 Strasbourg, France, Kluyver Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands, and Laboratoire de Cristallochimie, UMR 7513, Université Louis Pasteur, 4, rue Blaise Pascal, 67070 Strasbourg, France

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja016907u

Reference44 articles.

1. Effects of Concerted Hydrogen Bonding of Distal Histidine on Active Site Structures of Horseradish Peroxidase. Resonance Raman Studies with Asn70 Mutants

2. Structural properties of peroxidases

3. Cytochrome P450 cam : crystallography, oxygen activation, and electron transfer 1

4. Improvement of Peroxygenase Activity by Relocation of a Catalytic Histidine within the Active Site of Horseradish Peroxidase

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