Int. J. Mol. Sci. 2005, 6(9), 245-256; doi:10.3390/i6090245
Article

Inhibition of Heme Peroxidase During Phenol Derivatives Oxidation. Possible Molecular Cloaking of the Active Center

1,2,* email and 1
Received: 1 March 2005; Accepted: 29 August 2005 / Published: 20 October 2005
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: Ab initio quantum chemical calculations have been applied to the study of the molecular structure of phenol derivatives and oligomers produced during peroxidasecatalyzed oxidation. The interaction of substrates and oligomers with Arthromyces ramosus peroxidase was analyzed by docking methods. The most possible interaction site of oligomers is an active center of the peroxidase. The complexation energy increases with increasing oligomer length. However, the complexed oligomers do not form a precise (for the reaction) hydrogen bonding network in the active center of the enzyme. It seems likely that strong but non productive docking of the oligomers determines peroxidase inhibition during the reaction.
Keywords: Ab initio; docking; peroxidase; phenol; oligomer
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MDPI and ACS Style

Ziemys, A.; Kulys, J. Inhibition of Heme Peroxidase During Phenol Derivatives Oxidation. Possible Molecular Cloaking of the Active Center. Int. J. Mol. Sci. 2005, 6, 245-256.

AMA Style

Ziemys A, Kulys J. Inhibition of Heme Peroxidase During Phenol Derivatives Oxidation. Possible Molecular Cloaking of the Active Center. International Journal of Molecular Sciences. 2005; 6(9):245-256.

Chicago/Turabian Style

Ziemys, Arturas; Kulys, Juozas. 2005. "Inhibition of Heme Peroxidase During Phenol Derivatives Oxidation. Possible Molecular Cloaking of the Active Center." Int. J. Mol. Sci. 6, no. 9: 245-256.

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