Computational Study on Compound I Redox-Active Species in Horseradish Peroxydase Enzyme: Conformational Fluctuations and Solvation Effects-Reference-Cited by-同舟云学术

Computational Study on Compound I Redox-Active Species in Horseradish Peroxydase Enzyme: Conformational Fluctuations and Solvation Effects

Published:2010-05-03 Issue:20 Volume:114 Page:6817-6824
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Zazza Costantino¹,Palma Amedeo¹,Sanna Nico¹,Tatoli Simone¹,Aschi Massimiliano¹

Affiliation:

1. CASPUR, Consorzio Interuniversitario per le Applicazioni di Supercalcolo per Università e Ricerca, Via dei Tizii, 6/b, 00185 Roma, Italy, Istituto per lo Studio dei Materiali Nanostrutturati, CNR-ISMN, via Salaria Km. 29.3, Sez. Montelibretti, Monterotondo S.(RM), Italy, Dipartimento di Chimica, Università di Roma La Sapienza, P. le A. Moro 00185, Rome, Italy, and Dipartimento di Chimica, Ingegneria Chimica e Materiali, Universita di L’Aquila, via Vetoio 67100, L’Aquila, Italy

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp101033w

Reference50 articles.

1. Crystal structure of horseradish peroxidase C at 2.15 Å resolution

2. dMarnett, L. J.; Kennedy, T. A.InCytochrome P450: Structure, Mechanisms and Biochemistry,2nded.Ortiz de Montellano, P. R., Ed.Plenum Press:New York, 1995; pp49−80.

3. Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia)

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