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Biophysical Journal 67: 1713-1723 (1994)
© 1994 the Biophysical Society

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Stereodynamic properties of the cooperative homodimeric Scapharca inaequivalvis hemoglobin studied through optical absorption spectroscopy and ligand rebinding kinetics.

A Boffi, D Verzili, E Chiancone, M Leone, A Cupane, V Militello, E Vitrano, L Cordone, W Yu and E E Di Iorio

CNR Center of Molecular Biology, Department of Biochemical Sciences, University La Sapienza, Roma, Italy.

ABSTRACT

The study of the thermal evolution of the Soret band in heme proteins has proved to be a useful tool to understand their stereodynamic properties; moreover, it enables one to relate protein matrix fluctuations and functional behavior when carried out in combination with kinetic experiments on carbon monoxide rebinding after flash photolysis. In this work, we report the thermal evolution of the Soret band of deoxy, carbonmonoxy, and nitric oxide derivatives of the cooperative homodimeric Scapharca inaequivalvis hemoglobin in the temperature range 10-300 K and the carbon monoxide rebinding kinetics after flash photolysis in the temperature range 60-200 K. The two sets of results indicate that Scapharca hemoglobin has a very rigid protein structure compared with other hemeproteins. This feature is brought out i) by the absence of nonharmonic contributions to the soft modes coupled to the Soret band in the liganded derivatives, and ii) by the almost "in plane" position of the iron atom in the photoproduct obtained approximately 10(-8) s after dissociating the bound carbon monoxide molecule at 15 K.




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T. K. Das, A. Boffi, E. Chiancone, and D. L. Rousseau
Hydroxide Rather Than Histidine Is Coordinated to the Heme in Five-coordinate Ferric Scapharca inaequivalvis Hemoglobin
J. Biol. Chem., January 29, 1999; 274(5): 2916 - 2919.
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Copyright © 1994 by the Biophysical Society.