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Biophysical Journal 61: 750-755 (1992)
© 1992 the Biophysical Society

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A new mode for heme-heme interactions in hemoglobin associated with distal perturbations.

A Levy, V S Sharma, L Zhang and J M Rifkind

Molecular Dynamics Section, National Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224.

ABSTRACT

The distal side of the heme pocket, known to regulate ligand affinity, is shown to be directly involved in subunit interactions. Valency hybrids with oxygen or carbon monoxide bound to the reduced chain are used to model R-state hemoglobin with different distal perturbations. Electron paramagnetic resonance of the oxidized chains shows that the carbon monoxide perturbation is transmitted between subunits to the distal histidine and the oxidized iron center. A comparison of hybrids with only one type of chain oxidized and hybrids with a single alpha beta dimer oxidized is consistent with this perturbation being transmitted across the alpha 1 beta 1 interface. This represents a new mode of subunit interactions in hemoglobin.




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Copyright © 1992 by the Biophysical Society.