An initial review (PCET1) on proton-coupled electron transfer (PCET) by Huynh and Meyer
appeared in Chemical Reviews in 2007.(1) This is a follow-up on the original. It was …

Incorporation of metallocofactors essential for the activity of many enyzmes is a major
mechanism of posttranslational modification. The cellular machinery required for these …

How cells ensure correct metallation of a given protein and whether a degree of promiscuity
in metal binding has evolved are largely unanswered questions. In a classic case, iron-and …

Ribonucleotide reductases (RNRs) utilize radical chemistry to reduce nucleotides to
deoxynucleotides in all organisms. In the class Ia and Ib RNRs, this reaction requires a …

Metalloproteins with active sites containing di-Fe cores exhibit diverse chemical reactivity
that is linked to the precise transfer of protons and electrons which directly involve the di-Fe …

Enzymes that activate dioxygen at carboxylate-bridged non-heme diiron clusters residing
within ferritin-like, four-helix-bundle protein architectures have crucial roles in, among other …

The MbnBC enzyme complex converts cysteine residues in a peptide substrate, MbnA, to
oxazolone/thioamide groups during the biosynthesis of copper chelator methanobactin …

Ribonucleotide reductase (RNR) catalyzes the rate limiting step in DNA synthesis where
ribonucleotides are reduced to their corresponding deoxyribonucleotides. They are formed …

Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion
of nucleotides to deoxynucleotides and requires a diferric-tyrosyl radical (Y•) cofactor to …

A class Ia ribonucleotide reductase (RNR) employs a μ-oxo-Fe2III/III/tyrosyl radical cofactor
in its β subunit to oxidize a cysteine residue∼ 35 Å away in its α subunit; the resultant …