Wertz, Ashlee E. and Rosenkampff, Ilmari and Ibouanga, Philippe and Huber, Matthias and Hess, Corinna R. and Ruediger, Olaf and Shafaat, Hannah S. (2025) A semisynthetic, multicofactor artificial metalloenzyme retains independent site activity. JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 30 (1). pp. 13-23. ISSN 0949-8257, 1432-1327
Full text not available from this repository. (Request a copy)Abstract
Native metalloenzymes are unparalleled in their ability to perform efficient small molecule activation reactions, converting simple substrates into complex products. Most of these natural systems possess multiple metallocofactors to facilitate electron transfer or cascade catalysis. While the field of artificial metalloenzymes is growing at a rapid rate, examples of artificial enzymes that leverage two distinct cofactors remain scarce. In this work, we describe a new class of artificial enzymes containing two different metallocofactors, incorporated through bioorthogonal strategies. Nickel-substituted rubredoxin (NiRd), which is a structural and functional mimic of [NiFe] hydrogenases, is used as a scaffold. Incorporation of a synthetic bimetallic inorganic complex based on a macrocyclic biquinazoline ligand (MMBQ) was accomplished using a novel chelating thioether linker. Neither the structure of the NiRd active site nor the MMBQ were altered upon attachment, and each site retained independent redox activity. Electrocatalysis was observed from each site, with the switchability of the system demonstrated through the use of catalytically inert metal centers. This MMBQ-NiRd platform offers a new avenue to create multicofactor artificial metalloenzymes in a robust system that can be easily tuned both through modifications to the protein scaffold and the synthetic moiety, with applications for redox catalysis and tandem reactivity.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | OXYGEN-TOLERANT; NIFE HYDROGENASE; ELECTRON-TRANSFER; STRUCTURAL BASIS; CATALYTIC BIAS; 4FE-3S CLUSTER; COMPLEXES; REDOX; CHEMISTRY; RELEVANCE; Hydrogenase; Redox cofactor; Electron transfer; Bioorthogonal coupling; Electrocatalysis |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Anorganische Chemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 20 Apr 2026 11:40 |
| Last Modified: | 20 Apr 2026 11:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/67634 |
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