1 May 1993 Protein response to ligation reactions in myoglobin
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Proceedings Volume 1890, Biomolecular Spectroscopy III; (1993) https://doi.org/10.1117/12.145243
Event: OE/LASE'93: Optics, Electro-Optics, and Laser Applications in Scienceand Engineering, 1993, Los Angeles, CA, United States
Abstract
The protein response to the photodissociation, escape and subsequent rebinding of carbon monoxide in myoglobin is studied using time-resolved infrared (TRIR) spectroscopy. All phases of these reactions are investigated, from ultrafast phenomena (picoseconds) to relatively slow processes (milliseconds). Conformational changes in myoglobin (Mb) are detected by time-resolved infrared absorption changes in the amide I band. On the hundreds of nanoseconds to milliseconds timescale, a 'real-time' apparatus is used. This apparatus is based on a tunable diode laser operating in the region of 1650 cm-1. The time course of changes in the amide I band are shown to follow the recombination of CO with photolyzed Mb. On the basis of the rise times of the amide I and Fe-CO signals, it is concluded that protein motion is complete within 100 ns. A time-resolved difference spectrum in the amide I region is generated from single wavelength transients taken throughout the amide I envelope. A static difference spectrum is also generated by subtracting FTIR spectra of carbonmonoxy and deoxy myoglobin. The two difference spectra are compared and are interpreted in terms of the three-dimensional structures of deoxy and carbonmonoxy Mb. Preliminary picosecond TRIR data are also given for the ultrafast response of the protein immediately following photodissociation of CO.
© (1993) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Timothy P. Causgrove and R. Brian Dyer "Protein response to ligation reactions in myoglobin", Proc. SPIE 1890, Biomolecular Spectroscopy III, (1 May 1993); doi: 10.1117/12.145243; https://doi.org/10.1117/12.145243
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