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Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K

Nature Structural Biology volume 1, pages 701–705 (1994)Cite this article

Abstract

Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.

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Author notes

  1. T.-Y. Teng and V. Šrajer: These authors contributed equally to this work.

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, 60637, U.S.A.

    K. Moffat

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  1. T.-Y. Teng
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  2. V. Šrajer
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  3. K. Moffat
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Teng, TY., Šrajer, V. & Moffat, K. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nat Struct Mol Biol 1, 701–705 (1994). https://doi.org/10.1038/nsb1094-701

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