A click chemistry approach to site-specific immobilization of a small laccase enables efficient direct electron transfer in a biocathode

Guan, Dongli; Kurra, Yadagiri; Liu, Wenshe Ray; Chen, Zhilei

doi:10.1039/c4cc09179e

Cited by 46 publications

(49 citation statements)

References 32 publications

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“…Moreover, a unique alkyne chemical handle of ncAAs will ensure a covalent linkage of the mutated enzymes with the modified electrode via click chemistry [133]. By varying the length and position of the linker on the E. coli CueO, the distance of the enzyme's electroactive site relative to the glassy carbon electrode was controlled [134].…”

Section: Enzyme Engineeringmentioning

confidence: 99%

“…An attractive new strategy is the use of noncanonical amino acids (ncAAs) like propargyl-L-lysine (PrK), which can be genetically introduced at desired locations on the enzyme [133] (Figure 6). Moreover, a unique alkyne chemical handle of ncAAs will ensure a covalent linkage of the mutated enzymes with the modified electrode via click chemistry [133].…”

Section: Enzyme Engineeringmentioning

confidence: 99%

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Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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Abstract: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.

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Section: Enzyme Engineeringmentioning

confidence: 99%

Section: Enzyme Engineeringmentioning

confidence: 99%

Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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“…[14][15][16][17] When a conjugation site was carefully chosen, the enzyme retained the catalytic activity even after the conjugation. Once a clickable non-natural amino acid was introduced into enzymes, a click reaction, such as coppercatalyzed azide-alkyne cycloaddition (CuAAC) or SPAAC, was employed to immobilize enzymes onto the solid surface.…”

mentioning

confidence: 99%

Double clicking for site-specific coupling of multiple enzymes

2015

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“…Depending on the site of NNAA incorporation and the structure of a chemical linker, spatial orientation of a single protein towards a specific target as well as the geometry of macroscopic protein assembly can be controlled and customized in accordance with user-defined preferences404142. As a first step to construct FDH-MDH conjugates with their active sites in face-to-face (FF conjugate) or back-to-back orientation (BB conjugate) (Fig.…”

Section: Resultsmentioning

confidence: 99%

Controlled Orientation of Active Sites in a Nanostructured Multienzyme Complex

Lim

Yang

Jung

et al. 2016

Sci Rep

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Multistep cascade reactions in nature maximize reaction efficiency by co-assembling related enzymes. Such organization facilitates the processing of intermediates by downstream enzymes. Previously, the studies on multienzyme nanocomplexes assembled on DNA scaffolds demonstrated that closer interenzyme distance enhances the overall reaction efficiency. However, it remains unknown how the active site orientation controlled at nanoscale can have an effect on multienzyme reaction. Here, we show that controlled alignment of active sites promotes the multienzyme reaction efficiency. By genetic incorporation of a non-natural amino acid and two compatible bioorthogonal chemistries, we conjugated mannitol dehydrogenase to formate dehydrogenase with the defined active site arrangement with the residue-level accuracy. The study revealed that the multienzyme complex with the active sites directed towards each other exhibits four-fold higher relative efficiency enhancement in the cascade reaction and produces 60% more D-mannitol than the other complex with active sites directed away from each other.

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A click chemistry approach to site-specific immobilization of a small laccase enables efficient direct electron transfer in a biocathode

Cited by 46 publications

References 32 publications

Controlling Redox Enzyme Orientation at Planar Electrodes

Controlling Redox Enzyme Orientation at Planar Electrodes

Double clicking for site-specific coupling of multiple enzymes

Controlled Orientation of Active Sites in a Nanostructured Multienzyme Complex

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