The Bioorganometallic Chemistry of Hydrogenase Chapter uri icon

abstract

  • © 2015 Wiley-VCH Verlag GmbH & Co. KGaA. All rights reserved. A new subfield of bioorganometallic chemistry is evolving, which derives from hydrogenase enzymes: metalloproteins containing low-valent, first-row transition metals within metal-metal binding distance and stabilized by the most classical of organometallic ligands, carbon monoxide. The review of the structures, mechanisms, and synthetic analogs of the active sites of [NiFe]-, [FeFe]-, and [Fe]-hydrogenase enzymes recalls the discovery and characterization of such organometallics, well buried within proteins and required by some of the most ancient of organisms. Historically, the role of synthetic chemists in the study of enzymes has been largely directed toward providing structural and spectroscopic references for biochemists. The same is true with hydrogenases; however, with the obvious structures and reactivity in the active sites, organometallic chemists are moving forward with enzyme active site-inspired compounds that display catalytic function, both as small molecules in their own right and through incorporation into active enzymes. These are described in this chapter.

author list (cited authors)

  • Bethel, R. D., & Darensbourg, M. Y.

citation count

  • 2

Book Title

  • Bioorganometallic Chemistry

publication date

  • December 2014