Hemoglobin models, structures

VI. H NMR Investigations of Structures and Properties of Symmetric Valency Hybrid Hemoglobins Models for Doubly... 

The properties of individual hemoglobins are consequences of their quaternary as well as of their secondary and tertiary structures. The quaternary structure of hemoglobin confers striking additional properties, absent from monomeric myoglobin, which adapts it to its unique biologic roles. The allosteric (Gk alios other, steros space ) properties of hemoglobin provide, in addition, a model for understanding other allosteric proteins (see Chapter 11). 

STRUCTURE OF THE ACTIVE SITE IN MYOGLOBIN AND HEMOGLOBIN COMPARISON TO MODEL COMPOUNDS... 

Figure 4.12 Distal histidine hydrogen bonding structure for hemoglobin (left) and a heme model (right). (Reprinted with permission from Figure 12 of Momenteau, M. Reed, C. A. Chem. Rev., 1994, 94, 659-698. Copyright 1994, American Chemical Society.)...

Despite all these studies of proteins and synthetic models, many essential aspects of the function of myoglobin and hemoglobin, e.g. the way the protein controls the binding of ligands (02, CO, and NO), the precise structure of the Fe-ligand bonds and the structure-spin-energy relationships at the active center, are a topic of debate [2]. 

Structure of the Active Site in Myoglobin and Hemoglobin Comparison to Model Compounds... 

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