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PMID: 7647252 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Ligand binding to heme proteins. V. Light-induced relaxation in proximal mutants L89I and H97F of carbonmonoxymyoglobin.

Biophysical journal ·Vol. 68 ·No. 6 ·1995-06-00 ·Pages 2497-504

Abadan Y, Chien EY, Chu K, Eng CD, Nienhaus GU, Sligar SG

Abstract

We have studied the proximal mutants L89I and H97F of MbCO with FTIR and temperature-derivative spectroscopy at temperatures between 10 and 160 K. The mutations give rise only to minor alterations of the stretch spectra of the bound and photodissociated CO ligand. The most pronounced difference is a larger population in the A3 substate at approximately 1930 cm-1 in the mutants. The barrier distributions, as determined by temperature-derivative spectroscopy, are very similar to native MbCO after short illumination. Extended illumination leads to substantial increases of the rebinding barriers in native MbCO and the proximal mutants. A larger fraction of light-relaxed states is found in the proximal mutants, implying that the conformational energy landscape has been modified to more easily allow light-induced transitions. These and other spectroscopic data imply that the large changes in the binding properties are brought about by a light-induced conformational relaxation involving the structure at the heme iron. Similarities with spectral hole-burning studies and physical models are discussed.

MeSH Terms
Animals Hemeproteins/chemistry,metabolism Hydrogen-Ion Concentration Ligands Mutagenesis, Site-Directed Myoglobin/chemistry,metabolism Point Mutation Protein Conformation Spectroscopy, Fourier Transform Infrared/methods Whales
Chemicals
Hemeproteins Ligands Myoglobin carboxymyoglobin
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Abadan Y
Department of Physics, University of Illinois at Urbana-Champaign 61801, USA.
Chien E Y
Chu K
Eng C D
Nienhaus G U
Sligar S G
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1995-06-00
Pages
2497-504
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1282159
Subset
IM
Grants
NIGMS NIH HHS · GM 18051 · United States
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