Artificial Metalloenzymes Publications @Ward Group

2 publications

A Structural View of Synthetic Cofactor Integration into [FeFe]-Hydrogenases

Chem. Sci. 2016, 7, 959-968, 10.1039/C5SC03397G

Crystal structures of semisynthetic [FeFe]-hydrogenases with variations in the [2Fe] cluster show little structural differences despite strong effects on activity.

Metal: Fe

Ligand type: CN; CO; Dithiolate

Host protein: [FeFe]-hydrogenase from C. pasteurianum (CpI)

Anchoring strategy: Dative

Optimization: Chemical

Reaction: H2 evolution

Max TON: ---

ee: ---

PDB: 4XDC

Notes: H2 evolution activity of the ArM: 2874 (mmol H2)*min-1*(mg protein)-1.

Chalcogenide Substitution in the [2Fe] Cluster of [FeFe]-Hydrogenases Conserves High Enzymatic Activity

Apfel, U.-P.; Happe, T.

Dalton Trans. 2017, 46, 16947-16958, 10.1039/C7DT03785F

Combination of biological and chemical methods allow for creation of [FeFe]-hydrogenases with an artificial synthetic cofactor.