It was once widely held that nearly all reactions in biology were catalyzed via mechanisms
involving paired electron species. Beginning approximately 40 years ago, this paradigm was …

Molybdenum is the only second-row transition metal required by most living organisms, and
is nearly universally distributed in biology. Enzymes containing molybdenum in their active …

Radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex
and chemically challenging reactions across all domains of life. Of approximately 114,000 of …

Sactipeptides are ribosomally synthesized peptides that contain a characteristic thioether
bridge (sactionine bond) that is installed posttranslationally and is absolutely required for …

The radical SAM enzymes—also referred to as the AdoMet radical enzymes—are a newly
identified enzyme superfamily1 capable of catalyzing radical chemistry similar to, but more …

Molybdenum cofactor (Moco) biosynthesis is an ancient, ubiquitous, and highly conserved
pathway leading to the biochemical activation of molybdenum. Moco is the essential …

S-Adenosylmethionine (SAM, also known as AdoMet) radical enzymes use SAM and a [4Fe-
4S] cluster to catalyze a diverse array of reactions. They adopt a partial triose-phosphate …

Covering: up to the end of 2017 C–C bond formations are frequently the key steps in
cofactor and natural product biosynthesis. Historically, C–C bond formations were thought to …

A vast number of enzymes are now known to belong to a superfamily known as radical SAM,
which all contain a [4Fe–4S] cluster ligated by three cysteine residues. The remaining …

How living organisms create carbon-sulfur bonds during the biosynthesis of critical sulfur-
containing compounds is still poorly understood. The methylthiotransferases MiaB and …