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 …

The present article comprehensively reviews the macromolecular synthesis using enzymes
as catalysts. Among the six main classes of enzymes, the three classes, oxidoreductases …

Conspectus The remarkable aliphatic C–H hydroxylations catalyzed by the heme-containing
enzyme, cytochrome P450, have attracted sustained attention for more than four decades …

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 …

High-valent iron-oxo intermediates have often been implicated, and in some cases
identified, as the active oxidant in oxygen activating nonheme iron enzymes. Recent …

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 …

The title to a seminar presentation by IC Gunsalus in 1973 was “Oxygen: An essential toxin”,
referring to the complex role that atmospheric dioxygen has in biology. The relatively simple …

Direct C–H bond functionalization catalyzed by non-precious transition metals is an
attractive strategy in synthetic chemistry. Compared with the precious metals rhodium …

Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

This is the second set of Handbook of Porphyrin Science. Porphyrins, phthalocyanines and
their numerous analogues and derivatives are materials of tremendous importance in …