Sökning: WFRF:(Johnson Ben T.) > (2020-2024) > Mimicking the Elect...
Fältnamn | Indikatorer | Metadata |
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000 | 03867naa a2200385 4500 | |
001 | oai:DiVA.org:uu-448926 | |
003 | SwePub | |
008 | 210712s2021 | |||||||||||000 ||eng| | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4489262 URI |
024 | 7 | a https://doi.org/10.1021/jacs.1c013612 DOI |
040 | a (SwePub)uu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Castner, Ashleigh T.u Uppsala universitet,Syntetisk molekylär kemi4 aut0 (Swepub:uu)ashca734 |
245 | 1 0 | a Mimicking the Electron Transport Chain and Active Site of [FeFe] Hydrogenases in One Metal-Organic Framework :b Factors That Influence Charge Transport |
264 | c 2021-05-24 | |
264 | 1 | b American Chemical Society (ACS),c 2021 |
338 | a electronic2 rdacarrier | |
520 | a [FeFe] hydrogenase (H2ase) enzymes are effective proton reduction catalysts capable of forming molecular dihydrogen with a high turnover frequency at low overpotential. The active sites of these enzymes are buried within the protein structures, and substrates required for hydrogen evolution (both protons and electrons) are shuttled to the active sites through channels from the protein surface. Metal–organic frameworks (MOFs) provide a unique platform for mimicking such enzymes due to their inherent porosity which permits substrate diffusion and their structural tunability which allows for the incorporation of multiple functional linkers. Herein, we describe the preparation and characterization of a redox-active PCN-700-based MOF (PCN = porous coordination network) that features both a biomimetic model of the [FeFe] H2ase active site as well as a redox-active linker that acts as an electron mediator, thereby mimicking the function of [4Fe4S] clusters in the enzyme. Rigorous studies on the dual-functionalized MOF by cyclic voltammetry (CV) reveal similarities to the natural system but also important limitations in the MOF-enzyme analogy. Most importantly, and in contrast to the enzyme, restrictions apply to the total concentration of reduced linkers and charge-balancing counter cations that can be accommodated within the MOF. Successive charging of the MOF results in nonideal interactions between linkers and restricted mobility of charge-compensating redox-inactive counterions. Consequently, apparent diffusion coefficients are no longer constant, and expected redox features in the CVs of the materials are absent. Such nonlinear effects may play an important role in MOFs for (electro)catalytic applications. | |
650 | 7 | a NATURVETENSKAPx Kemix Organisk kemi0 (SwePub)104052 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Chemical Sciencesx Organic Chemistry0 (SwePub)104052 hsv//eng |
650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
700 | 1 | a Johnson, Ben A.u Uppsala universitet,Syntetisk molekylär kemi4 aut0 (Swepub:uu)benjo679 |
700 | 1 | a Cohen, Seth M.u Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92023 USA4 aut |
700 | 1 | a Ott, Saschau Uppsala universitet,Syntetisk molekylär kemi4 aut0 (Swepub:uu)saott499 |
710 | 2 | a Uppsala universitetb Syntetisk molekylär kemi4 org |
773 | 0 | t Journal of the American Chemical Societyd : American Chemical Society (ACS)g 143:21, s. 7991-7999q 143:21<7991-7999x 0002-7863x 1520-5126 |
856 | 4 | u https://doi.org/10.1021/jacs.1c01361y Fulltext |
856 | 4 | u https://uu.diva-portal.org/smash/get/diva2:1579887/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print |
856 | 4 | u https://pubs.acs.org/doi/pdf/10.1021/jacs.1c01361 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-448926 |
856 | 4 8 | u https://doi.org/10.1021/jacs.1c01361 |
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