Journal Article
Proceedings of the National Academy of Sciences, vol. 111, iss. 46, pp. 16286-16291, 2014
Authors
Arnab Dutta, Daniel L. DuBois, John A. S. Roberts, Wendy J. Shaw
Abstract
Significance
Enzymes achieve rapid and reversible H
2
oxidation catalysis by cooperative behavior between the active site and the protein scaffold. To better understand the role of the enzyme scaffold, we have attached amino acids (glycine, arginine, and arginine methyl ester) to an active functional mimic of hydrogenase to give
[
Ni
(
P
2
Cy
N
2
Amino
acid
)
2
]
2
+
. The resulting complexes are fully reversible catalysts with the arginine complex exhibiting high activity for both H
2
oxidation/production, functionality achieved by the addition of an outer coordination sphere.
