On the basis of its generally accessible I/II redox couple and bioavailability, copper plays a
wide variety of roles in nature that mostly involve electron transfer (ET), O 2 binding …

Nature uses dioxygen as a key oxidant in the transformation of biomolecules. Among the
enzymes that are utilized for these reactions are copper-containing metalloenzymes, which …

Mononuclear non-heme ferrous iron dependent oxygenases and oxidases constitute an
extended enzyme family that catalyze a wide range of oxidation reactions. The largest …

Ring-cleaving dioxygenases catalyze key reactions in the aerobic microbial degradation of
aromatic compounds. Many pathways converge to catecholic intermediates, which are …

Cysteine dioxygenase (CDO) is a vital enzyme for human health involved in the
biodegradation of toxic cysteine and thereby regulation of the cysteine concentration in the …

Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid.
Deficiencies in this enzyme have been linked to autoimmune diseases and neurological …

Cysteine dioxygenase is a mononuclear iron-dependent enzyme responsible for the
oxidation of cysteine with molecular oxygen to form cysteine sulfinate. This reaction commits …

The catalytic functions of metalloenzymes are often strongly correlated with metal elements
in the active sites. However, dioxygen-activating nonheme quercetin dioxygenases (QueD) …

Mononuclear, non-heme-Fe (II) centers are key structures in O2 metabolism and catalyze an
impressive variety of enzymatic reactions. While most are bound via two histidines and a …

Cysteine dioxygenase (CDO) catalyzes the oxidation of cysteine to cysteine sulfinic acid,
which is the first major step in cysteine catabolism in mammalian tissues. Crystal structures …