Comparison of QM-only and QM/MM models for the mechanism of tyrosinase
2011 (English)In: Faraday discussions (Online), ISSN 1364-5498, E-ISSN 1359-6640, Vol. 148, 109-117 p.Article in journal (Refereed) Published
Two previous studies on the mechanism of tyrosinase have given quite conflicting results. In a QM-only study using a rather small model, a mechanism was suggested in which the tyrosine proton is removed before catalysis. This was followed by catalytic cycles where a superoxo ligand attacks the phenolate ring. In another, more recent study, at the QM/MM level including the entire protein in the model, a quite different mechanism was instead advocated where a bridging O(2)H ligand was homolytically cleaved. That mechanism was rejected in the earlier QM-only study as having a prohibitively large barrier for O-O bond cleavage. In the present study, this discrepancy between the previous studies is investigated by new QM-only and QM/MM calculations.
Place, publisher, year, edition, pages
2011. Vol. 148, 109-117 p.
IdentifiersURN: urn:nbn:se:su:diva-69705DOI: 10.1039/c004378hISI: 000285361500008OAI: oai:DiVA.org:su-69705DiVA: diva2:478008
authorCount :22012-01-152012-01-152012-01-15Bibliographically approved