In our mimicry of biological dioxygen binding by hemoglobin and myoglobin, we have proven by pulse EPR methods the existence of a H-bond in Co(II)-oxymyoglobin as well as in model complexes 1 -Co-O2 and 2 -Co-O2.[1] Our current efforts in this field are focused on the investigation of the H-bond strength by systematically varying the N�H acidity of the distal base in the model complex 1 -Co-O2. Our most recent results towards this goal are presented.   [1]  a) H. Dube, B. Kasumaj, C. Calle, M. Saito, G. Jeschke, F. Diederich, Angew. Chem. Int. Ed. 2008 , 47, 2600�2603;  b) H. Dube, B. Kasumaj, C. Calle, B. Felber, M. Saito, G. Jeschke, F. Diederich, Chem. Eur. J. 2009 , 15, 125�135.

Exploring the role and strength of the H-bond in model systems for hemoglobin and myoglobin

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.