Design of a Functional Nitric Oxide Reductase within a Myoglobin Scaffold

Köhler, Valentin and Ward, Thomas R.. (2010) Design of a Functional Nitric Oxide Reductase within a Myoglobin Scaffold. Chembiochem : a European journal of chemical biology, 118 (8). pp. 81049-81051.

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Official URL: http://edoc.unibas.ch/dok/A5841555

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A review. In recent years, significant progress has been made in the computational design of functional artificial enzymes. When combined with directed evolution protocols, their efficiencies are comparable to those obtained with catalytic antibodies. In comparison, the in silico creation of artificial metalloenzymes remains challenging. This could be due to the difficulty in computing both the transition states for metal-catalyzed reactions and the corresponding entatic state for a metalloenzyme. In a recent study, structurally characterized a functional bacterial nitric oxide reductase within a myoglobin scaffold has been rationally designed. This ground-breaking study by Lu and coworkers has opened the way towards the rational design of artificial metalloenzymes for more challenging reactions. For the artificial nitric oxide reductase, several issues deserve further scrutiny: catalytic efficiency as well as detailed reaction mechanism. In a broader perspective, the use of more elaborate computational algorithms, combined with efficient directed-evolution protocols should enable the creation and optimization of highly versatile artificial metalloenzymes in a variety of protein folds. [on SciFinder(R)]
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Ward, Thomas R. R. and Köhler, Valentin
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:24 Aug 2023 11:07
Deposited On:14 Sep 2012 07:00

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