A growing subset of metalloenzymes activates dioxygen with nonheme diiron active sites to
effect substrate oxidations that range from the hydroxylation of methane and the …

The natural amino acid hypusine (N δ-4-amino-2-hydroxybutyl (lysine)) is derived from the
polyamine spermidine, and occurs only in a single family of cellular proteins, eukaryotic …

BesC catalyzes the iron-and O2-dependent cleavage of 4-chloro-l-lysine to form 4-chloro-l-
allylglycine, formaldehyde, and ammonia. This process is a critical step for a biosynthetic …

Abstract Hypusine [N ε-(4-amino-2-hydroxybutyl) lysine] is a derivative of lysine that is
formed post-translationally in the eukaryotic initiation factor 5A (eIF5A). Its occurrence at a …

In biosynthesis of the pancreatic cancer drug streptozotocin, the tridomain nonheme-iron
oxygenase SznF hydroxylates N δ and N ω′ of N ω-methyl-l-arginine before oxidatively …

X-ray structures of homopolymeric L-ferritin obtained by freezing protein crystals at
increasing exposure times to a ferrous solution showed the progressive formation of a triiron …

Discovery of soluble methane monooxygenase (sMMO) in 1966 aroused enthusiastic
research on dinuclear iron centers, both in biological systems and chemical models. From …

Organophosphonate (Pn) catabolism constitutes the major source of inorganic phosphate
(Pi), which is essential for the synthesis of genetic and cellular components. Unlike various …

Binuclear non-heme iron enzymes activate O2 for diverse chemistries that include
oxygenation of organic substrates and hydrogen atom abstraction. This process often …

The final step in the biosynthesis of the antibiotic chloramphenicol is the oxidation of an aryl-
amine substrate to an aryl-nitro product catalyzed by the N-oxygenase CmlI in three two …