The reaction takes place at a specialized metal center that dramatically increases the acidity
of H2 and leads to a heterolytic splitting of the molecule which is strongly accelerated by the …

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 …

Abstract The [FeFe]-and [NiFe]-hydrogenases catalyze the formal interconversion between
hydrogen and protons and electrons, possess characteristic non-protein ligands at their …

Conspectus The seeds for recognition of the vast superfamily of radical S-adenosyl-l-
methionine (SAM) enzymes were sown in the 1960s, when Joachim Knappe found that the …

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 …

Hydrogenases use complex metal cofactors to catalyze the reversible formation of hydrogen.
In [FeFe]-hydrogenases, the H-cluster cofactor includes a diiron subcluster containing …

Radical S-adenosyl-l-methionine (SAM) enzymes comprise a vast superfamily catalyzing
diverse reactions essential to all life through homolytic SAM cleavage to liberate the highly …

Nature uses multinuclear metal clusters to catalyse a number of important multielectron
redox reactions. Examples that employ complex Fe–S clusters in catalysis include the Fe …

[FeFe] hydrogenases carry out the redox interconversion of protons and molecular hydrogen
(2H++ 2e−⇌ H2) at a complex Fe–S active site known as the H-cluster. The H-cluster …

Conspectus Nature's prototypical hydrogen-forming catalysts─ hydrogenases─ have
attracted much attention because they catalyze hydrogen evolution at near zero …