Mechanism of Enzyme Binding Hydrogen Gas

Mechanism of Enzyme Binding Hydrogen Gas

Author: Angewandte Chemie International Edition

A research team led by Seigo Shima, Max-Planck-Institute for Terrestrial Microbiology, Germany, has successfully applied iron-chromophore circular dichroism (CD) spectroscopy to probe the mechanism of an enzyme that binds hydrogen gas, thereby confirming predictions from crystal structures of the protein.

[Fe]-hydrogenase, which contains a unique iron cofactor (FeGP cofactor), catalyzes the reversible hydrogenation of methenyltetrahydrometanopterin (methenyl-H4MPT+) with H2 to methylene-H4MPT (see scheme). The CD data support the hypothesis that the binding of methenyl/methylene-H4MPT induces a conformational change that closes the active-site cleft of [Fe]-hydrogenase to form the intact active site.


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