Nature endows life with a wide variety of sophisticated, synergistic, and highly functional
protein assemblies. Following Nature's inspiration to assemble protein building blocks into …

Tyrosine hydroxylase is the rate-limiting enzyme of catecholamine biosynthesis; it uses
tetrahydrobiopterin and molecular oxygen to convert tyrosine to DOPA. Its amino terminal …

There have been significant advances in our understanding of mononuclear nonheme iron
oxygenases since our 1996 Chemical Reviews article, 1 promoted in large part by the many …

In recent years, significant progress has been made in understanding the geometric and
electronic structures of the active sites of non-heme iron enzymes and the contributions of …

Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the biosynthesis of dopamine
(DA) and other catecholamines, and its dysfunction leads to DA deficiency and …

Accumulating evidence suggests that α-synuclein (α-syn) occurs physiologically as a
helically folded tetramer that resists aggregation. However, the mechanisms underlying the …

▪ Abstract Phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase
constitute a small family of monooxygenases that utilize tetrahydropterins as substrates …

Iron-containing enzymes are one of Nature's main means of effecting key biological
transformations. The mononuclear non-heme iron oxygenases and oxidases have received …

Aerobic life on our planet relies on the use of molecular oxygen for energy as well as for
biosynthesis of important biological compounds in metabolic pathways. Thermodynamically …

A 2‐His‐1‐carboxylate facial triad is a common feature of the active sites in a number of
mononuclear non‐heme iron (II) enzymes. This structural motif was established …