As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply
of metalloproteins for oxidative metabolism and protection against reactive oxygen species …

Activation and reduction of O2 and H2O2 by synthetic and biosynthetic iron porphyrin
models have proved to be a versatile platform for evaluating second-sphere effects deemed …

Enzymes are complex biological catalysts and are critical to life. Most oxidations of
chemicals are catalyzed by cytochrome P450 (P450, CYP) enzymes, which generally utilize …

Membrane proteins play a most important part in metabolism, signaling, cell motility,
transport, development, and many other biochemical and biophysical processes which …

Two decades ago, theoretical model calculations played a truly minor role in understanding
mechanisms of redox-active metalloenzymes. The methods available to treat transition …

Since our initial report in 1976, the oxygen rebound mechanism has become the consensus
mechanistic feature for an expanding variety of enzymatic C–H functionalization reactions …

Cytochrome P450 enzymes are responsible for the phase I metabolism of approximately
75% of known pharmaceuticals. P450s perform this and other important biological functions …

Metalloporphyrins are widely used throughout the biosphere, and of these heme (iron
protoporphyrin IX, Figure 1) is one of the most abundant and widely used. Heme shuttles …

In chemical terms, the regio-and stereoselective hydroxylation of hydrocarbon CH bonds is a
very difficult transformation. Nevertheless, these reactions are deftly catalyzed by a variety of …

The introduction of oxygen into biochemical processes has brought about an evolutionary
leap in the history of life, whereby many organisms have evolved to use oxygen as part of …