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Crystal structure of photolysed carbonmonoxy-myoglobin

Nature volume 371, pages 808–812 (1994)Cite this article

Abstract

MYOGLOBIN is a globular haem protein that reversibly binds lig-ands such as O2 and CO. Single photons of visible light can break the covalent bond between CO and the haem iron in carbonmonoxy-myoglobin (MbCO) and thus form an unstable intermediate, Mb*CO, with the CO inside the protein1,2. The ensuing rebinding process has been extensively studied as a model for the interplay of dynamics, structure and function in protein reactions. We have used X-ray crystallography at liquid-helium temperatures to determine the structure of Mb*CO to a resolution of 1.5 Å. The photodissociated CO lies on top of the haem pyrrole ring C. Comparison with the CO-bound and unligated myoglobin structures reveals that on photodissociation of the CO, the haem 'domes', the iron moves partially out of the haem plane, the iron–proximal histidine bond is compressed, the F helix is strained and the distal histidine swings towards the outside of the ligand-binding pocket.

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Authors and Affiliations

  1. Department of Biophysics, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120, Heidelberg, Germany

    Ilme Schlichting

  2. Department of Biochemistry and Cell Biology and the W.M. Keck Center for Computational Biology, Rice University, Houston, Texas, 77251–1892, USA

    George N. Phillips Jr

  3. Biology Department, Brookhaven National Laboratory, Upton, New York, 11973, USA

    Robert M. Sweet

Authors
  1. Ilme Schlichting
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  2. Joel Berendzen
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  3. George N. Phillips Jr
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  4. Robert M. Sweet
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Schlichting, I., Berendzen, J., Phillips, G. et al. Crystal structure of photolysed carbonmonoxy-myoglobin. Nature 371, 808–812 (1994). https://doi.org/10.1038/371808a0

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