Metalloenzymes catalyze a variety of reactions using a limited number of natural amino
acids and metallocofactors. Therefore, the environment beyond the primary coordination …

Conspectus Despite the astonishing diversity of naturally occurring biocatalytic processes,
enzymes do not catalyze many of the transformations favored by synthetic chemists. Either …

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 …

Enzymes that catalyze carbon–silicon bond formation are unknown in nature, despite the
natural abundance of both elements. Such enzymes would expand the catalytic repertoire of …

Although abundant in organic molecules, carbon–hydrogen (C–H) bonds are typically
considered unreactive and unavailable for chemical manipulation. Recent advances in C–H …

Highlights•Engineered hemoproteins expand the biocatalytic repertoire.•Different
hemoprotein scaffolds offer diverse activities and selectivities.•New enzymes enable …

Recent advances in enzyme engineering and design have expanded nature's catalytic
repertoire to functions that are new to biology,,. However, only a subset of these engineered …

Iron is an especially important redox-active cofactor in biology because of its ability to
mediate reactions with atmospheric O2. Iron-dependent oxygenases exploit this earth …

Many oxidation–reduction (redox) enzymes, particularly oxygenases, have roles in reactions
that make and break C–C bonds. The list includes cytochrome P450 and other heme-based …

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