Many efforts are being made in the design and engineering of metalloenzymes with catalytic properties fulfilling the needs of practical applications. Progress in this field has recently been accelerated by advances in computational, molecular and structural biology. This review article focuses on the recent examples of oxygen-activating metalloenzymes, developed through the strategies of de novo design, miniaturization processes and protein redesign. Considerable progress in these diverse design approaches has produced many metal-containing biocatalysts able to adopt the functions of native enzymes or even novel functions beyond those found in Nature.
|Original language||English (US)|
|Number of pages||35|
|Journal||Chemical Society Reviews|
|State||Published - Sep 21 2016|
Bibliographical noteFunding Information:
We wish to thank all coworkers and collegues for their contributions to the results described in this review, as well as Fabrizia Sibillo for help with editing the manuscript. The work from the authors' groups reported herein has been supported by US National Institutes of Health (GM062211), US National Science Foundation (CHE 14-13328), the European Union (EU) (Cost Action CM1003 Biological Oxidation Reactions: Mechanisms and Design of New Catalysts) and the Scientific Research Department of Campania Region (BIP Project, POR FESR 2007/2013, grant number B25C13000290007, and the STRAIN Project, POR FSE 2007/2013, grant number B25B0900000000 for a postdoctoral fellowship to M. C.)
© The Royal Society of Chemistry 2016.