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Controlling Redox Enzyme Orientation at Planar Electrodes

National Center for Scientific Research (CNRS), Aix Marseille University, BIP, UMR 7281, 31 Chemin Aiguier, 13009 Marseille, France
Laboratoire de Biochimie Théorique, National Center for Scientific Research (CNRS), UPR9080, Université Paris Diderot, Sorbonne Paris Cité, PSL Research University, 13 rue Pierre et Marie Curie, 75005 Paris, France
Chemistry and Biology of Membranes and Nanoobjects, UMR 5248 CNRS, University of Bordeaux, Bat. B14 allée Geoffroy St. Hilaire, 33600 Pessac, France
Author to whom correspondence should be addressed.
Catalysts 2018, 8(5), 192;
Received: 13 April 2018 / Revised: 27 April 2018 / Accepted: 28 April 2018 / Published: 4 May 2018
(This article belongs to the Special Issue Immobilized Biocatalysts)
Redox enzymes, which catalyze reactions involving electron transfers in living organisms, are very promising components of biotechnological devices, and can be envisioned for sensing applications as well as for energy conversion. In this context, one of the most significant challenges is to achieve efficient direct electron transfer by tunneling between enzymes and conductive surfaces. Based on various examples of bioelectrochemical studies described in the recent literature, this review discusses the issue of enzyme immobilization at planar electrode interfaces. The fundamental importance of controlling enzyme orientation, how to obtain such orientation, and how it can be verified experimentally or by modeling are the three main directions explored. Since redox enzymes are sizable proteins with anisotropic properties, achieving their functional immobilization requires a specific and controlled orientation on the electrode surface. All the factors influenced by this orientation are described, ranging from electronic conductivity to efficiency of substrate supply. The specificities of the enzymatic molecule, surface properties, and dipole moment, which in turn influence the orientation, are introduced. Various ways of ensuring functional immobilization through tuning of both the enzyme and the electrode surface are then described. Finally, the review deals with analytical techniques that have enabled characterization and quantification of successful achievement of the desired orientation. The rich contributions of electrochemistry, spectroscopy (especially infrared spectroscopy), modeling, and microscopy are featured, along with their limitations. View Full-Text
Keywords: metalloenzymes; enzyme immobilization; enzyme orientation; electrodes; bioelectrocatalysis metalloenzymes; enzyme immobilization; enzyme orientation; electrodes; bioelectrocatalysis
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MDPI and ACS Style

Hitaishi, V.P.; Clement, R.; Bourassin, N.; Baaden, M.; De Poulpiquet, A.; Sacquin-Mora, S.; Ciaccafava, A.; Lojou, E. Controlling Redox Enzyme Orientation at Planar Electrodes. Catalysts 2018, 8, 192.

AMA Style

Hitaishi VP, Clement R, Bourassin N, Baaden M, De Poulpiquet A, Sacquin-Mora S, Ciaccafava A, Lojou E. Controlling Redox Enzyme Orientation at Planar Electrodes. Catalysts. 2018; 8(5):192.

Chicago/Turabian Style

Hitaishi, Vivek P., Romain Clement, Nicolas Bourassin, Marc Baaden, Anne De Poulpiquet, Sophie Sacquin-Mora, Alexandre Ciaccafava, and Elisabeth Lojou. 2018. "Controlling Redox Enzyme Orientation at Planar Electrodes" Catalysts 8, no. 5: 192.

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