1126144-10-2

Upstream product

• 1033224-47-3 (((CH₃CH₂OOCCH₂CH₂CH₂O)2C₆H₃)2(C₇H₅N₂CC(C₃H₃N₂(CH₂)6O)C₆H₃)C₂₀H₉N₄)Co 
• 80937-33-3 oxygen 
• 1033224-47-3 C₈₀H₈₂CoN₈O₁₃ 

Relevant academic research and scientific papers

Probing hydrogen bonding to bound dioxygen in synthetic models for heme proteins: The importance of precise geometry

Distal hydrogen bonding in natural dioxygen binding proteins is crucial for the discrimination between different potential ligands such as O2 or CO. In the present study, we probe the chemical requirements for proper distal hydrogen bonding in a series of synthetic model compounds for dioxygen-binding heme proteins. The model compounds 1-Co to 7-Co bear different distal residues. The hydrogen bonding in their corresponding dioxygen adducts is directly measured by pulse EPR spectroscopy. The geometrical requirements for this interaction to take place were found to be narrow and very specific. Only two model complexes, 1-Co and 7-Co, form a hydrogen bond to bound dioxygen, which was characterized in terms of geometry and nature of the bond. The geometry and dipolar nature of this interaction in 1-Co-O2 is more similar to the one in natural cobalt myoglobin (Co-Mb), making 1-Co the best model compound in the entire series.

Direct evidence for a hydrogen bond to bound dioxygen in a myoglobin/hemoglobin model system and in cobalt myoglobin by pulse-EPR spectroscopy

(Figure Presented) Hydrogen bond revealed: In a cobalt(II) porphyrin complex which serves as a model for the dioxygen binding site of myoglobin (Mb) and hemoglobin, a distal hydrogen bond to the bound O2 was identified and characterized by pulse ENDOR spectroscopy. A similar but stronger hydrogen bond was revealed with the same methods in natural Co-Mb-O2.