Ribonucleotide reductases (RNRs) catalyze the de novo conversion of nucleotides to
deoxynucleotides in all organisms, controlling their relative ratios and abundance. In doing …

Genetic code expansion is a promising genetic engineering technology that incorporates
noncanonical amino acids into proteins alongside the natural set of 20 amino acids. This …

Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to
deoxyribonucleotides, thereby playing a key role in DNA replication and repair. Escherichia …

Some oxidoreductase enzymes use redox-active tyrosine, tryptophan, cysteine, and/or
glycine residues as one-electron, high-potential redox (radical) cofactors. Amino-acid radical …

Important bioactive natural products, including prostaglandin H2 and artemisinin, contain
reactive endoperoxides. Known enzymatic pathways for endoperoxide installation require …

Conspectus Many artificial enzymes that catalyze redox reactions have important energy,
environmental, and medical applications. Native metalloenzymes use a set of redox-active …

Both controllable regulation of the conformational structure of a polypeptide and specific
recognition of an amino acid are still arduous challenges. Here, a novel dual-mode …

The proton-coupled electron transfer (PCET) reactions of tyrosine (Y) are instrumental to
many redox reactions in nature. This study investigates how the local environment and the …

Proton-coupled electron transfer (PCET) from tyrosine produces a neutral tyrosyl radical (Y•)
that is vital to many catalytic redox reactions. To better understand how the protein …

The mechanistic enzymology of oxidoreductases has contributed to the development of
therapeutics, biomimetic synthetic catalysts, and engineered enzymes with improved or …