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Catalytic roles of active-site residues in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: an ONIOM/DFT study
National University of Ireland, Galway, Ireland. (Biofysikalisk kemi)
Örebro University, School of Science and Technology. (Biokemi)ORCID iD: 0000-0003-3315-8835
National University of Ireland, Galway, Ireland. (Biofysikalisk kemi)
2011 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 115, no 8, p. 1918-1926Article in journal (Refereed) Published
Abstract [en]

The catalytic mechanism of 2-methyl-3-hydroxypyridine-5-carboxylic acid (MHPC) oxygenase (MHPCO) has been systematically studied using DFT and ONIOM(DFT:MM) methods. MHPCO catalyzes the hydroxylation and subsequent ring-opening of the aromatic substrate MHPC to give the aliphatic product R-(N-acetylaminomethylene)succinic acid (AAMS). Our calculations show that the active-site residues Arg211 and Tyr223 have a minor effect on the reaction, while the peptide bond of Pro295-Ala296, the side chain of Tyr82 and several crystal water molecules affect the reaction energy profile considerably. Both DFT and ONIOM calculations show that the ring-opening pathway B, in which an epoxy transition state is formed, is more favored than the direct C2-C3 cleavage pathway A. Different QM/MM partitioning schemes have been used to study the enzymatic reaction, and the results show that both the reaction barriers for the hydroxylation and the ring-opening pathways are sensitive to the QM/MM partitioning.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2011. Vol. 115, no 8, p. 1918-1926
National Category
Physical Chemistry
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:oru:diva-15764DOI: 10.1021/jp111525pISI: 000287636700024OAI: oai:DiVA.org:oru-15764DiVA, id: diva2:420541
Available from: 2012-08-07 Created: 2011-06-01 Last updated: 2018-05-03Bibliographically approved

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Strid, Åke

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