Conformational Substates of the Oxyheme Centers in α and β Subunits of Hemoglobin As Disclosed by EPR and ENDOR Studies of Cryoreduced Protein
Copyright policy )Conformational Substates of the Oxyheme Centers in α and β Subunits of Hemoglobin As Disclosed by EPR and ENDOR Studies of Cryoreduced Protein
Exposure of frozen solutions of oxyhemoglobin to gamma-irradiation at 77 K yields EPR- and ENDOR-active, one-electron-reduced oxyheme centers which retain the conformation of the diamagnetic precursor. EPR spectra have been collected for the centers produced in human HbO(2) and isolated alphaO(2) and betaO(2) chains, as well as alphaO(2)beta(Zn), alpha(Zn)betaO(2), and alphaO(2)beta(Fe(3+)) hybrids, each in frozen buffer and in frozen glasses that form in the presence of glycols and sugars and also in the presence of IHP. These reveal two spectroscopically distinct classes of such ferriheme centers (g(1)
- Northwestern University United States
- University at Buffalo, State University of New York United States
- State University of New York at Potsdam United States
Oxygen, Hemoglobins, Protein Subunits, Myoglobin, Protein Conformation, Electron Spin Resonance Spectroscopy, Humans, Heme, Oxidation-Reduction
Oxygen, Hemoglobins, Protein Subunits, Myoglobin, Protein Conformation, Electron Spin Resonance Spectroscopy, Humans, Heme, Oxidation-Reduction
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