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Science 24 February 1984:
Vol. 223. no. 4638, pp. 811 - 813
DOI: 10.1126/science.223.4638.811
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Articles

Time-Resolved X-ray Absorption Spectroscopy of Carbon Monoxide-Myoglobin Recombination After Laser Photolysis

D. M. MILLS 1, A. LEWIS 2, A. HAROOTUNIAN 2, J. HUANG 2, and B. SMITH 2

1 Cornell High Energy Synchrotron Source, Cornell University, Ithaca, New York 14853
2 School of Applied and Engineering Physics, Cornell University

Results are presented for the first time-resolved x-ray absorption measurements with a time resolution of 300 microseconds on a dynamically evolving chemical system. By synchronizing a neodymium: yttrium-aluminum-garnet pulsed laser with the bursts of x-rays emitted from the Cornell High Energy Synchrotron Source, it was possible to monitor at room temperature the recombination of carbon monoxide with myoglobin after laser photolysis. Changes in the pre-edge structure and in the position of the iron edge of this protein were detected as a function of time.

Submitted on August 26, 1983
Accepted on December 19, 1983


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Structures of bromoalkanes' photodissociation in solution by means of ultrafast extended x-ray absorption fine-structure spectroscopy.
D. A. Oulianov, I. V. Tomov, A. S. Dvornikov, and P. M. Rentzepis (2002)
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Capturing a Photoexcited Molecular Structure Through Time-Domain X-ray Absorption Fine Structure.
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