A protein-derived cofactor is a catalytic or redox-active site in a protein that is formed by post-
translational modification of one or more amino acid residues. These post-translational …

Bacterial diheme peroxidases represent a diverse enzyme family with functions that range
from hydrogen peroxide (H2O2) reduction to post-translational modifications. By …

Neisseria gonorrhoeae is an obligate human pathogenic bacterium responsible for
gonorrhea, a sexually transmitted disease. The bacterial peroxidase, an enzyme present in …

The high-valent state of the diheme enzyme MauG exhibits charge–resonance (CR)
stabilization in which the major species is a bis-FeIV state with one heme present as FeIV …

In the absence of its substrate, the auto-reduction of the high-valent bis-Fe (IV) state of the
dihaem enzyme MauG is coupled to oxidative damage of a methionine residue. Transient …

Methanobactins (Mbns) are ribosomally-produced, post-translationally modified peptidic
copper-binding natural products produced under conditions of copper limitation. Genes …

The diheme cytochrome c peroxidase from Shewanella oneidensis (So CcP) requires a
single electron reduction to convert the oxidized, as-isolated enzyme to an active …

In the absence of its substrate, the autoreduction of the high-valent bis-FeIV state of the
hemes of MauG to the diferric state proceeds via a Compound I-like and then a Compound II …

The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational
modification of a precursor of methylamine dehydrogenase (preMADH) to complete the …

The diheme enzyme MauG catalyzes oxidative post‐translational modifications of a protein
substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the …