Year: 2025
Type: article
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. Graphical abstract
Institutions: The Ohio State University, Max Planck Institute for Chemical Energy Conversion, Centre National de la Recherche Scientifique, Université Paris-Saclay, Institut de Chimie Moléculaire et des Matériaux d'Orsay, Technical University of Munich, University of Regensburg, University of California, Los Angeles
Language: English
Field: Energy
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,990
Awards: EXC 2089: econversion, NSF-DFG EChem: CAS: Mechanistic Interrogation of Electrocatalytic Hydrogen Evolution by an Artificial Hydrogenase, NSF-DFG EChem: CAS: Mechanistic Interrogation of Electrocatalytic Hydrogen Evolution by an Artificial Hydrogenase, NSF Echem: Mechanistische Untersuchung der elektrokatalytischen Wasserstoffbildung durch eine künstliche Hydrogenase
OpenAlex ID: W4407056257