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J Biol Chem, Vol. 274, Issue 43, 30357-30360, October 22, 1999
From the Department of Physiology and Biophysics, Albert Einstein
College of Medicine, Bronx, New York 10461
We report for the first time specific
conformational changes for a homogeneous population of ligand-bound
adult deoxy human hemoglobin A (HbA) generated by introducing CO into a
sample of deoxy-HbA with the effector, inositol hexaphosphate,
encapsulated in a porous sol-gel. The preparation of ligand-bound
deoxy-HbA results from the speed of ligand diffusion relative to globin conformational dynamics within the sol-gel (1). The ultraviolet resonance Raman (UVRR) difference spectra obtained reveal that E helix
motion is initiated upon ligand binding, as signaled by the appearance
of an 
14
15 Trp W3 band difference at 1559 cm
1. The subsequent appearance of Tyr (Y8a and Y9a)
and W3 (1549 cm1) UVRR difference bands suggest
conformational shifts for the penultimate Tyr140 on the F helix, the
"switch" region Tyr42, and the "hinge" region Trp37. The
UVRR results expose a sequence of conformational steps leading up to
the ligation-induced T to R quaternary structure transition as opposed
to a single, concerted switch. More generally, this report demonstrates
that sol-gel encapsulation of proteins can be used to study a sequence
of specific conformational events triggered by substrate binding
because the traditional limitation of substrate diffusion times is overcome.
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