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On Dioxygen Permeation of MaL Laccase from the Thermophilic Fungus Melanocarpus albomyces : An all‐Atom Molecular Dynamics Investigation
Author(s) -
Pietra Francesco
Publication year - 2016
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.201600062
Subject(s) - laccase , chemistry , molecular dynamics , molecule , solvent , catalysis , atom (system on chip) , chemical physics , active site , computational chemistry , enzyme , stereochemistry , organic chemistry , embedded system , computer science
In this article, biased molecular dynamics ( MD ) simulations of O 2 egress from the active center of MaL laccase toward the bulk solvent were described. Parameterization of the set of four Cu( II ) ions, in the framework of CHARMM ‐36 FF , was carried out on a recent dummy‐atom model that takes into account the Jahn – Teller effect. By carrying out a number of statistically relevant MD simulations, under a tiny randomly oriented external force applied to the molecule O 2 , three preferred gates for O 2 egress from the enzyme and a few intermediate binding pockets ( BP s) for O 2 were visible; all the gates and pockets were located on two of the three domains. This wide distribution of preferred gates notwithstanding the molecule O 2 was seen to follow specific pathways, exploiting consistently the interstices created by the enzyme thermal fluctuations. These are features that can be imagined to have evolved to make MaL laccase extremely efficient as catalysts in various reactions that require O 2 .