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Conformational Dynamics Associated With Ligand Binding To Vertebrate Hexa-Coordinate Hemoglobins, Luisana Astudillo Mar 2014

Conformational Dynamics Associated With Ligand Binding To Vertebrate Hexa-Coordinate Hemoglobins, Luisana Astudillo

FIU Electronic Theses and Dissertations

Neuroglobin (Ngb) and cytoglobin (Cygb) are two new additions to the globin family, exhibiting heme iron hexa-coordination, a disulfide bond and large internal cavities. These proteins are implicated in cytoprotection under hypoxic-ischemic conditions, but the molecular basis of their cytoprotective function is unclear.

Herein, a photothermal and spectroscopic study of the interactions of diatomic ligands with Ngb, Cygb, myoglobin and hemoglobin is presented. The impact of the disulfide bond in Ngb and Cygb and role of conserved residues in Ngb His64, Val68, Cys55, Cys120 and Tyr44 on conformational dynamics associated with ligand binding/dissociation were investigated. Transient absorption and photoacoustic calorimetry …