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J. Biol. Chem., Vol. 277, Issue 28, 25783-25790, July 12, 2002
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From the Department of Physiology and Biophysics, Albert Einstein
College of Medicine, Bronx, New York 10461
We have used sol-gel encapsulation protocols to
trap kinetically and spectroscopically distinct conformational
populations of native horse carbonmonoxy myoglobin. The method
allows for direct comparison of functional and spectroscopic properties
of equilibrium and non-equilibrium populations under the same
temperature and viscosity conditions. The results implicate tertiary
structure changes that include the proximal heme environment in the
mechanism for population-specific differences in the observed rebinding kinetics. Differences in the resonance Raman frequency of
Spectroscopically and Kinetically Distinct
Conformational Populations of Sol-Gel-encapsulated Carbonmonoxy
Myoglobin
A COMPARISON WITH HEMOGLOBIN*
, and
(Fe-His), the iron-proximal histidine stretching mode, are attributed to differences in the positioning of the F helix. For myoglobin, the
degree of separation between the F helix and the heme is assigned as
the conformational coordinate that modulates both this frequency and
the innermost barrier controlling CO rebinding. A comparison with the
behavior of encapsulated derivatives of human adult hemoglobin indicates that these CO binding-induced conformational changes are
qualitatively similar to the tertiary changes that occur within both
the R and T quaternary states. Protein-specific differences in the time
scale for the proposed F helix relaxation are attributed to variations
in the intra-helical hydrogen bonding patterns that help stabilize the
position of the F helix.
*
This work was supported by National Institutes of Health
Grants RO1 HL65188, PO1 GM58890, and RO1 HL58247 and by the W. M. Keck
Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Chemistry, Bowdoin College, Brunswick,
ME 04011.
§
To whom correspondence should be addressed: Dept. of Physiology and
Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Ave.,
Bronx, NY 10461. Tel.: 718-430-3591; Fax: 718-430-8819; E-mail:
jfriedma@aecom.yu.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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