Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin

Kelvin Chu, Jaroslav Vojtchovský, Benjamin H. McMahon, Robert M. Sweet, Joel Berendzen and Ilme Schlichting ()
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Kelvin Chu: P-21 Biophysics Group, MS-D454, Los Alamos National Laboratory
Jaroslav Vojtchovský: Max Planck Institute for Molecular Physiology
Benjamin H. McMahon: Center for Nonlinear Studies, Los Alamos National Laboratory
Robert M. Sweet: Department of Biology Brookhaven National Laboratory
Joel Berendzen: Cook Building University of Vermont
Ilme Schlichting: Max Planck Institute for Molecular Physiology

Nature, 2000, vol. 403, issue 6772, 921-923

Abstract: Abstract Small molecules such as NO, O2, CO or H2 are important biological ligands that bind to metalloproteins to function crucially in processes such as signal transduction, respiration and catalysis. A key issue for understanding the regulation of reaction mechanisms in these systems is whether ligands gain access to the binding sites through specific channels and docking sites, or by random diffusion through the protein matrix. A model system for studying this issue is myoglobin, a simple haem protein. Myoglobin has been studied extensively by spectroscopy, crystallography, computation and theory1,2,3,4,5,6,7,8,9,10,11. It serves as an aid to oxygen diffusion but also binds carbon monoxide, a byproduct of endogenous haem catabolism. Molecular dynamics simulations3,4,5, random mutagenesis6 and flash photolysis studies7,8,9,10 indicate that ligand migration occurs through a limited number of pathways involving docking sites. Here we report the 1.4 Å resolution crystal structure of a ligand-binding intermediate in carbonmonoxy myoglobin that may have far-reaching implications for understanding the dynamics of ligand binding and catalysis.

Date: 2000
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DOI: 10.1038/35002641

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