A versatile artificial metalloenzyme scaffold enabling direct bioelectrocatalysis in solution.

Artificial metalloenzymes (ArMs) are commonly designed with protein scaffolds containing buried coordination pockets to achieve substrate specificity and product selectivity for homogeneous reactions. However, their reactivities toward heterogeneous transformations are limited because interfacial electron transfers are hampered by the backbone shells. Here, we introduce bacterial small laccase (SLAC) as a new protein scaffold for constructing ArMs to directly catalyze electrochemical transformations.

Role of rare-earth elements in enhancing bioelectrocatalysis for biosensing with NAD-dependent glutamate dehydrogenase.

Dehydrogenases (DHs) are widely explored bioelectrocatalysts in the development of enzymatic bioelectronics like biosensors and biofuel cells. However, the relatively low intrinsic reaction rates of DHs which mostly depend on diffusional coenzymes (, NAD) have limited their bioelectrocatalytic performance in applications such as biosensors with a high sensitivity. In this study, we find that rare-earth elements (REEs) can enhance the activity of NAD-dependent glutamate dehydrogenase (GDH) toward highly sensitive electrochemical biosensing of glutamate .

Natural Leukocyte Membrane-Masked Microelectrodes with an Enhanced Antifouling Ability and Biocompatibility for Electrochemical Sensing.

Probing chemical information in the central nervous system is essential for understanding the molecular mechanism of brain function. Electrochemistry with tissue-implantable carbon fiber electrodes (CFEs) provides a powerful tool for monitoring the dynamics of neurochemicals in a subsecond time scale; however, the implantation of CFEs into brain tissue immediately causes the nonspecific adsorption of proteins on electrode surfaces. This process can dramatically impact the performance of the electrochemical method in terms of reduced sensitivity and accuracy.

Identification of Flavin Mononucleotide as a Cell-Active Artificial N -Methyladenosine RNA Demethylase.

N -Methyladenosine (m A) represents a common and highly dynamic modification in eukaryotic RNA that affects various cellular pathways. Natural dioxygenases such as FTO and ALKBH5 are enzymes that demethylate m A residues in mRNA. Herein, the first identification of a small-molecule modulator that functions as an artificial m A demethylase is reported.

Nanoscale ATP-Responsive Zeolitic Imidazole Framework-90 as a General Platform for Cytosolic Protein Delivery and Genome Editing.

Metal-organic frameworks (MOFs) are an emerging class of nanocarriers for drug delivery, owing to their tunable chemical functionality. Here we report ATP-responsive zeolitic imidazole framework-90 (ZIF-90) as a general platform for cytosolic protein delivery and CRISPR/Cas9 genome editing. The self-assembly of imidazole-2-carboxaldehyde and Zn with protein forms ZIF-90/protein nanoparticles and efficiently encapsulates protein.

A single-atom Fe-N catalytic site mimicking bifunctional antioxidative enzymes for oxidative stress cytoprotection.

Atomically dispersed Fe-N4 sites anchored on N-doped porous carbon materials (Fe-SAs/NC) can mimic two antioxidative enzymes of catalase (CAT) and superoxide dismutase (SOD), and therefore serves as a bifunctional single-atom-based enzyme (SAzyme) for scavenging reactive oxygen species (ROS) to remove excess ROS generated during oxidative stress in cells.

Exploring Ferredoxin-Dependent Glutamate Synthase as an Enzymatic Bioelectrocatalyst.

Ferredoxin-dependent glutamate synthase (Fd-GltS) is reported as an enzymatic bioelectrocatalyst for the first time. By configuring mediated electrochemical interfaces with mediators of different redox potentials, we realize bioelectrosynthesis or bioelectrooxidation of glutamate with recombinant Fd-GltS from cyanobacteria. Particularly, bioelectrocatalytic oxidation of glutamate by Fd-GltS is demonstrated to be oxygen independent.