uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Oxoferryl species in mononuclear non-heme iron enzymes: biosynthesis, properties and reactivity from a theoretical perspective
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Theoretical Chemistry.
2013 (English)In: Coordination chemistry reviews, ISSN 0010-8545, E-ISSN 1873-3840, Vol. 257, no 1, 277-289 p.Article, review/survey (Refereed) Published
Abstract [en]

Mononuclear non-heme iron enzymes perform a wide range of chemical reactions. Still, the catalytic mechanisms are usually remarkably similar, with formation of a key oxoferryl (Fe(IV)=O) intermediate through two well-defined steps. First, two-electron reduction of dioxygen occurs to form a peroxo species, followed by O-O bond cleavage. Even though the peroxo species have different chemical character in various enzyme families, the analogies between different enzymes in the group make it an excellent base for investigating factors that control metal-enzyme catalysis. We have used density-functional theory to model the complete chemical reaction mechanisms of several enzymes, e.g., for aromatic and aliphatic hydroxylation, chlorination, and oxidative ring-closure. Reactivity of the Fe(IV)=O species is discussed with focus on electronic and steric factors determining the preferred reaction path. Various spin states are compared, as well as the two reaction channels that stem from involvement of different frontier molecular orbitals of Fe(IV)=O. Further, the two distinctive species of Fe(IV)=O, revealed by Mossbauer spectroscopy, and possibly relevant for specificity of aliphatic chlorination, can be identified. The stability of the modeling results have been analyzed using a range of approaches, from active-site models to multi-scale models that include classical free-energy contributions. Large effects from an explicit treatment of the protein matrix (similar to 10 kcal/mol) can be observed for O-2 binding, electron-transfer and product release.

Place, publisher, year, edition, pages
2013. Vol. 257, no 1, 277-289 p.
Keyword [en]
Enzyme catalysis; Non-heme iron; O-O bond cleavage, Oxoferryl, Density-functional theory, Multi-scale modeling
National Category
Theoretical Chemistry
URN: urn:nbn:se:uu:diva-181244DOI: 10.1016/j.ccr.2012.03.047ISI: 000312972700022OAI: oai:DiVA.org:uu-181244DiVA: diva2:555497
Available from: 2012-09-20 Created: 2012-09-20 Last updated: 2013-02-06Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full texthttp://dx.doi.org/10.1016/j.ccr.2012.03.047

Search in DiVA

By author/editor
Lundberg, Marcus
By organisation
Theoretical Chemistry
In the same journal
Coordination chemistry reviews
Theoretical Chemistry

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 403 hits
ReferencesLink to record
Permanent link

Direct link