Stabilization of synthetic heme-superoxo complexes by hydrogen bonding: a still on-going quest

Author:

Boitrel Bernard1234ORCID,Le Gac Stéphane1234ORCID

Affiliation:

1. UMR CNRS 6226

2. Institut des Sciences Chimiques de Rennes, Université de Rennes 1

3. 35042 Rennes cedex

4. France

Abstract

The design of various types of synthetic heme models has allowed the fine tuning of the location of hydrogen bond donors around the ferrous coordination site. Through the years, it has migrated from a lateral to a quasi-apical position. Still, the unambiguous existence of an actual H-bond with the dioxygen adduct remains to be established.

Funder

Centre National de la Recherche Scientifique

Ministère de l'Education Nationale, de l'Enseignement Superieur et de la Recherche

Agence Nationale de la Recherche

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,General Chemistry,Catalysis

Reference31 articles.

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2. G. B. Jameson and J. A.Ibers , Biological and Synthetic Dioxygen Carriers , in Bioinorganic Chemistry , ed. I. Bertini , H. B. Gray , E. I. Stiefel and J. S. Valentine , University Science Books , Mill Valley, California , 1994 , pp. 354–388

3. Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand

4. Nature of the Fe−O2 Bonding in Oxy-Myoglobin: Effect of the Protein

5. Regulating the Coordination State of a Heme Protein by a Designed Distal Hydrogen-Bonding Network

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