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Neutron diffraction study of carbonmonoxymyoglobin.

X D Cheng1, B P Schoenborn

  • 1Department of Biology, Brookhaven National Laboratory, Upton, NY 11973.

Journal of Molecular Biology
|July 20, 1991
PubMed
Summary

Neutron diffraction revealed distorted carbonmonoxide (CO) binding in myoglobin, with the distal histidine deprotonated and a water molecule bound. This study details the precise atomic structure and interactions within the myoglobin crystal.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Crystallography

Background:

  • Myoglobin is a crucial protein for oxygen transport.
  • Understanding ligand binding is key to protein function.
  • Neutron diffraction provides unique insights into hydrogen atom positions.

Purpose of the Study:

  • To determine the precise atomic structure of carbonmonoxymyoglobin using neutron diffraction.
  • To elucidate the binding conformation of the carbon monoxide (CO) ligand.
  • To investigate the protonation states and hydrogen bonding networks within the protein.

Main Methods:

  • Neutron diffraction data collection from a carbonmonoxymyoglobin crystal.
  • Refinement using the PROLSQ (restrained least-squares procedure in reciprocal space) method.

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  • Solvent analysis technique to model ordered solvent molecules.

    • Main Results:

    • The carbon monoxide (CO) ligand adopted two distorted, non-linear binding conformations.
    • The distal histidine residue was found to be deprotonated, with a water molecule bound to its N delta atom.
    • Specific hydrogen bonding interactions were identified, including between Arg45 and Asp60, and the heme propionic acid groups.
    • The heme group was found to be nearly planar.
    • Analysis of hydrogen atom exchange revealed specific main-chain amide hydrogens involved in stable hydrogen bonds.

    Conclusions:

    • The study provides a high-resolution structural model of carbonmonoxymyoglobin, revealing details of ligand binding and protein-ligand interactions.
    • The observed distortions in CO binding and the protonation state of distal histidine offer insights into the mechanism of ligand binding and release.
    • The detailed hydrogen bonding network and solvent interactions highlight the importance of the surrounding environment in stabilizing the protein structure and function.