Photolysis of the Carbon Monoxide Complex of Myoglobin:
Nanosecond Time-Resolved Crystallography
Vukica 
rajer,
Tsu-yi Teng,
Thomas Ursby,
Claude Pradervand,
Zhong Ren,
Shin-ichi Adachi,
Wilfried Schildkamp,
Dominique Bourgeois,
Michael Wulff,
Keith Moffat
*
The biological activity of macromolecules is accompanied by rapid
structural changes. The photosensitivity of the carbon monoxide complex
of myoglobin was used at the European Synchrotron Radiation Facility to
obtain pulsed, Laue x-ray diffraction data with nanosecond time
resolution during the process of heme and protein relaxation after
carbon monoxide photodissociation and during rebinding. These
time-resolved experiments reveal the structures of myoglobin photoproducts, provide a structural foundation to spectroscopic results
and molecular dynamics calculations, and demonstrate that time-resolved
macromolecular crystallography can elucidate the structural bases of
biochemical mechanisms on the nanosecond time scale.
V. rajer, T.-y. Teng, C. Pradervand, Z. Ren, W. Schildkamp,
K. Moffat, Department of Biochemistry and Molecular Biology and the
Consortium for Advanced Radiation Sources, The University of Chicago,
Chicago, IL 60637, USA.
T. Ursby and M. Wulff, European Synchrotron Radiation Facility (ESRF),
38043 Grenoble Cedex, France.
S.-i. Adachi, Biophysical Chemistry Laboratory, Institute of Physical
and Chemical Research, Saitama 351-01, Japan.
D. Bourgeois, UPR 9015/IBS, 38027 Grenoble, France, and ESRF, 38043 Grenoble Cedex, France.
*
To whom correspondence should be addressed.
