How to Build a Metalloenzyme: Lessons from a Protein-Based Model of Acetyl Coenzyme A Synthase.

"What I cannot create, I do not understand"─Richard Feynman. This sentiment motivates the entire field of artificial metalloenzymes. Naturally occurring enzymes catalyze reactions with efficiencies, rates, and selectivity that generally cannot be achieved in synthetic systems.

Thioester synthesis by a designed nickel enzyme models prebiotic energy conversion.

The formation of carbon-carbon bonds from prebiotic precursors such as carbon dioxide represents the foundation of all primordial life processes. In extant organisms, this reaction is carried out by the carbon monoxide dehydrogenase (CODH)/acetyl coenzyme A synthase (ACS) enzyme, which performs the cornerstone reaction in the ancient Wood-Ljungdahl metabolic pathway to synthesize the key biological metabolite, acetyl-CoA. Despite its significance, a fundamental understanding of this transformation is lacking, hampering efforts to harness analogous chemistry.

Controlling the Direction of -Nitrosation versus Denitrosation: Reversible Cleavage and Formation of an S-N Bond within a Dicopper Center.

Iron and copper enzymes are known to promote reversible -nitrosation/denitrosation in biology. However, it is unclear how the direction of S-N bond formation/scission is controlled. Herein, we demonstrate the interconversion of metal--nitrosothiol adduct M(RSNO) and metal nitrosyl thiolate complex M(NO)(SR), which may regulate the direction of reversible -(de)nitrosation.