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Protein response to ligation reactions in myoglobin

Conference ·

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 areinvestigated, from ultrafast phenomena (picoseconds) to relatively slow processes (milliseconds). Conformational changes in myoglobin (Mb) are detected by time-resolved 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[sup [minus]1] . The time course ofchanges 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 n. 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.

Research Organization:
Los Alamos National Lab., NM (United States)
Sponsoring Organization:
DOE; DOHHS; USDOE, Washington, DC (United States); Department of Health and Human Services, Washington, DC (United States)
DOE Contract Number:
W-7405-ENG-36
OSTI ID:
6708071
Report Number(s):
LA-UR-92-572; CONF-930159--18; ON: DE93008700; CNN: GM48509; X15B
Country of Publication:
United States
Language:
English