Electrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores
In living cells, redox chains rely on nanoconfinement using tiny enclosures, such as the mitochondrial matrix or chloroplast stroma, to concentrate enzymes and limit distances that nicotinamide cofactors and other metabolites must diffuse. In a chemical analogue exploiting this principle, nicotinami...
Main Authors: | , , , , , , , , , , , |
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Format: | Journal article |
Language: | English |
Published: |
Wiley
2019
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_version_ | 1797069948621684736 |
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author | Megarity, CF Siritanaratkul, B Heath, RS Wan, L Morello, G Fitzpatrick, SR Booth, RL Sills, AJ Robertson, AW Warner, JH Turner, NJ Armstrong, FA |
author_facet | Megarity, CF Siritanaratkul, B Heath, RS Wan, L Morello, G Fitzpatrick, SR Booth, RL Sills, AJ Robertson, AW Warner, JH Turner, NJ Armstrong, FA |
author_sort | Megarity, CF |
collection | OXFORD |
description | In living cells, redox chains rely on nanoconfinement using tiny enclosures, such as the mitochondrial matrix or chloroplast stroma, to concentrate enzymes and limit distances that nicotinamide cofactors and other metabolites must diffuse. In a chemical analogue exploiting this principle, nicotinamide adenine dinucleotide phosphate (NADPH) and NADP+ are cycled rapidly between ferredoxin-NADP+ reductase and a second enzyme-the pairs being juxtaposed within the 5-100 nm scale pores of an indium tin oxide electrode. The resulting electrode material, denoted (FNR+E2)@ITO/support, can drive and exploit a potentially large number of enzyme-catalysed reactions. |
first_indexed | 2024-03-06T22:31:57Z |
format | Journal article |
id | oxford-uuid:5892c175-86c3-4e69-afa6-24cddd26843a |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T22:31:57Z |
publishDate | 2019 |
publisher | Wiley |
record_format | dspace |
spelling | oxford-uuid:5892c175-86c3-4e69-afa6-24cddd26843a2022-03-26T17:04:21ZElectrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode poresJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5892c175-86c3-4e69-afa6-24cddd26843aEnglishSymplectic Elements at OxfordWiley2019Megarity, CFSiritanaratkul, BHeath, RSWan, LMorello, GFitzpatrick, SRBooth, RLSills, AJRobertson, AWWarner, JHTurner, NJArmstrong, FAIn living cells, redox chains rely on nanoconfinement using tiny enclosures, such as the mitochondrial matrix or chloroplast stroma, to concentrate enzymes and limit distances that nicotinamide cofactors and other metabolites must diffuse. In a chemical analogue exploiting this principle, nicotinamide adenine dinucleotide phosphate (NADPH) and NADP+ are cycled rapidly between ferredoxin-NADP+ reductase and a second enzyme-the pairs being juxtaposed within the 5-100 nm scale pores of an indium tin oxide electrode. The resulting electrode material, denoted (FNR+E2)@ITO/support, can drive and exploit a potentially large number of enzyme-catalysed reactions. |
spellingShingle | Megarity, CF Siritanaratkul, B Heath, RS Wan, L Morello, G Fitzpatrick, SR Booth, RL Sills, AJ Robertson, AW Warner, JH Turner, NJ Armstrong, FA Electrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores |
title | Electrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores |
title_full | Electrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores |
title_fullStr | Electrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores |
title_full_unstemmed | Electrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores |
title_short | Electrocatalytic volleyball: rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores |
title_sort | electrocatalytic volleyball rapid nanoconfined nicotinamide cycling for organic synthesis in electrode pores |
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