Interactive biocatalysis achieved by driving enzyme cascades inside a porous conducting material
Open Access
- 10 June 2024
- journal article
- review article
- Published by Springer Nature in Communications Chemistry
- Vol. 7 (1) , 1-11
Abstract
An emerging concept and platform, the electrochemical Leaf (e-Leaf), offers a radical change in the way tandem (multi-step) catalysis by enzyme cascades is studied and exploited. The various enzymes are loaded into an electronically conducting porous material composed of metallic oxide nanoparticles, where they achieve high concentration and crowding – in the latter respect the environment resembles that found in living cells. By exploiting efficient electron tunneling between the nanoparticles and one of the enzymes, the e-Leaf enables the user to interact directly with complex networks, rendering simultaneous the abilities to energise, control and observe catalysis. Because dispersion of intermediates is physically suppressed, the output of the cascade – the rate of flow of chemical steps and information – is delivered in real time as electrical current. Myriad enzymes of all major classes now become effectively electroactive in a technology that offers scalability between micro-(analytical, multiplex) and macro-(synthesis) levels. This Perspective describes how the e-Leaf was discovered, the steps in its development so far, and the outlook for future research and applications.Keywords
Funding Information
- RCUK | Biotechnology and Biological Sciences Research Council (BB/P023797/1)
This publication has 79 references indexed in Scilit:
- Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymesProceedings of the National Academy of Sciences, 2011
- Structural and mechanistic aspects of flavoproteins: photosynthetic electron transfer from photosystem I to NADP+The FEBS Journal, 2009
- Size and Shape of Protein Molecules at the Nanometer Level Determined by Sedimentation, Gel Filtration, and Electron MicroscopyBiological Procedures Online, 2009
- The degree of macromolecular crowding in the cytoplasm and nucleoplasm of mammalian cells is conservedFEBS Letters, 2007
- Macromolecular crowdingCurrent Biology, 2006
- Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observationsJournal of Pharmaceutical Sciences, 2005
- Enzyme Electrokinetics: Using Protein Film Voltammetry To Investigate Redox Enzymes and Their MechanismsBiochemistry, 2003
- Open questions in ferredoxin‐NADP+ reductase catalytic mechanismEuropean Journal of Biochemistry, 2003
- Competition between C-terminal Tyrosine and Nicotinamide Modulates Pyridine Nucleotide Affinity and Specificity in Plant Ferredoxin-NADP+ ReductaseJournal of Biological Chemistry, 2000
- A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies.Nature Structural & Molecular Biology, 1999