The cytochrome P450 monooxygenases (P450s) are thiolate heme proteins that can, often
under physiological conditions, catalyze many distinct oxidative transformations on a wide …

Understanding the redox cycling of metal ions in natural and biomimetic systems for
dioxygen activation in catalytic oxidation processes at the molecular level has stood at the …

The heme unit is one of the most ubiquitous and versatile cofactors found in Nature. 1, 2 The
amazingly diverse reactivities displayed by heme-dependent enzymes (eg, O2 transport and …

Oxyl radical character in the Mn O group of the title system is shown from a density
functional theory study to be essential for efficient C− H cleavage, which is a key step in C …

In natural systems, reactivity of iron is regulated by interactions with axial donor ligands. We
have designed a new synthetic route to a novel iron complex, CrCrFe (dpa) 4Cl2 (1, dpa= 2 …

1. INTRODUCTION Heme proteins are among the most versatile players in the biological
milieu; their functions range widely and include electron transfer, catalysis, and small …

“Click” reaction has been utilized to synthesize porphyrin ligands possessing distal
superstructures functionalized with ferrocenes, carboxylic acid esters, and phenols. Both …

The multifunctional enzyme, cytochrome P450 (CYP17A1), plays a crucial role in the
production of androgens, catalyzing two key reactions on pregnenolone (PREG) and …

We report herein a new molecular catalyst for efficient water splitting, aluminum porphyrins
(tetra‐methylpyridiniumylporphyrinatealuminum: AlTMPyP), containing earth's most …

Iron porphyrin complex with a covalently attached thiolate ligand and another with a
covalently attached phenolate ligand has been synthesized. The thiolate bound complex …