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On CO Egress from, and Re‐Uptake by, the Enzyme MauG, as a Mimic of the Acquisition of Oxidizing Agents by the pre‐MADH_MauG System. A Molecular Mechanics Approach
Author(s) -
Pietra Francesco
Publication year - 2012
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.201200176
Subject(s) - chemistry , heme , molecule , oxidizing agent , molecular dynamics , biophysics , transmembrane protein , ligand (biochemistry) , crystallography , enzyme , computational chemistry , biochemistry , receptor , organic chemistry , biology
In this work, by applying a non‐deterministic, randomly‐oriented minimal force to the dissociated CO ligand of the MauG‐CO system, the molecular‐dynamics (MD) behavior of this system could be quickly unraveled. It turned out that CO has no marked directional egress from the high‐spin c‐heme iron distal pocket. Rather, CO is able to exploit all interstices created during the protein fluctuations. Nonetheless, no steady route toward the surrounding solvent was ever observed: CO jumped first into other binding pockets before being able to escape the protein. In a few cases, on hitting the surrounding H 2 O molecules, CO was observed to reverse direction, re‐entering the protein. A contention that conformational inversion of the P107 ring provides a gate to the iron ion is not supported by the present simulations.