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Main Title: Enzymes as modular catalysts for redox halfreactions in H2-powered chemical synthesis: from biology to technology
Author(s): Reeve, Holly A.
Ash, Philip A.
Park, HyunSeo
Huang, Ailun
Posidias, Michalis
Tomlinson, Chloe
Lenz, Oliver
Vincent, Kylie A.
Type: Article
Language Code: en
Abstract: The present study considers the ways in which redox enzyme modules are coupled in living cells for linking reductive and oxidative half-reactions, and then reviews examples in which this concept can be exploited technologically in applications of coupled enzyme pairs. We discuss many examples in which enzymes are interfaced with electronically conductive particles to build up heterogeneous catalytic systems in an approach which could be termed synthetic biochemistry. We focus on reactions involving the H+/H2 redox couple catalysed by NiFe hydrogenase moieties in conjunction with other biocatalysed reactions to assemble systems directed towards synthesis of specialised chemicals, chemical building blocks or bio-derived fuel molecules. We review our work in which this approach is applied in designing enzyme-modified particles for H2-driven recycling of the nicotinamide cofactor NADH to provide a clean cofactor source for applications of NADH-dependent enzymes in chemical synthesis, presenting a combination of published and new work on these systems. We also consider related photobiocatalytic approaches for light-driven production of chemicals or H2 as a fuel. We emphasise the techniques available for understanding detailed catalytic properties of the enzymes responsible for individual redox half-reactions, and the importance of a fundamental understanding of the enzyme characteristics in enabling effective applications of redox biocatalysis.
Issue Date: 6-Jan-2017
Date Available: 14-Jun-2018
DDC Class: 547 Organische Chemie
Subject(s): biotechnology
heterogeneous catalysis
redox enzymes
Journal Title: Biochemical Journal
Publisher: Portland Press
Publisher Place: London
Volume: 474
Issue: 2
Publisher DOI: 10.1042/BCJ20160513
Page Start: 215
Page End: 230
EISSN: 1470-8728
ISSN: 0264-6021
Appears in Collections:Inst. Chemie » Publications

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