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N-O bond cleavage mechanism(s) in nitrous oxide reductase
Stockholm University, Faculty of Science, Department of Organic Chemistry.
Stockholm University, Faculty of Science, Department of Organic Chemistry.
2012 (English)In: Journal of Biological Inorganic Chemistry, ISSN 0949-8257, E-ISSN 1432-1327, Vol. 17, no 5, 687-698 p.Article in journal (Refereed) Published
Abstract [en]

Quantum chemical calculations of active-site models of nitrous oxide reductase (N2OR) have been undertaken to elucidate the mechanism of N-O bond cleavage mediated by the supported tetranuclear Cu4S core (Cu-Z) found in the enzymatic active site. Using either a minimal model previously employed by Gorelsky et al. (J. Am. Chem. Soc. 128:278-290, 2006) or a more extended model including key residue side chains in the active-site second shell, we found two distinct mechanisms. In the first model, N2O binds to the fully reduced Cu-Z in a bent mu-(1,3)-O,N bridging fashion between the Cu-I and Cu-IV centers and subsequently extrudes N-2 while generating the corresponding bridged mu-oxo species. In the second model, substrate N2O binds loosely to one of the coppers of Cu-Z in a terminal fashion, i.e., using only the oxygen atom; loss of N-2 generates the same mu-oxo copper core. The free energies of activation predicted for these two alternative pathways are sufficiently close to one another that theory does not provide decisive support for one over the other, posing an interesting problem with respect to experiments that might be designed to distinguish between the two. Effects of nearby residues and active-site water molecules are also explored.

Place, publisher, year, edition, pages
2012. Vol. 17, no 5, 687-698 p.
Keyword [en]
Density functional theory, Molecular modeling, Electronic structure, Transition state
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-79884DOI: 10.1007/s00775-012-0888-xISI: 000304566400002OAI: diva2:551847
Swedish Research Council


Available from: 2012-09-12 Created: 2012-09-11 Last updated: 2012-09-28Bibliographically approved

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Himo, FahmiSiegbahn, Per E. M.
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