Nanosecond step-scan FTIR spectroscopy applied to photobiological systems

Details Nanosecond step-scan FTIR spectroscopy applied to photobiological systems Nanosecond step-scan FTIR spectroscopy applied to photobiological systems

Jun 1998

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1998aipc..430..361r&link_type=abstract

The eleventh international conference on fourier transform spectroscopy. AIP Conference Proceedings, Volume 430, pp. 361-366 (1

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1

Spectra, Photodissociation, And Photoionization, Luminescence, Infrared And Raman Spectroscopy

Scientific paper

Our improved step-scan FTIR instrument, capable of measuring spectra within 15 ns after the flash, is employed to measure flash-induced infrared difference spectra of bacteriorhodopsin, halorhodopsin and CO-myoglobin. For all three systems it is necessary to cover a large time range extending into several milliseconds. Therefore, the linear time base provided by the transient recorder board is converted to a quasi-logarithmic scale. Each of the three systems is characterized by several time constants extending over the large time range. For bacteriorhodopsin, it is shown that two spectral changes occur, one in the 20 and the other in the 100 ns time range. Furthermore, spectral differences between the two M states could be detected in the μs time range. For halorhodopsin, a clear batho intermediate with red-shifted ethylenic mode could be identified in the nanosecond time range. In addition, a transition corresponding to the N intermediate in bacteriorhodopsin was deduced. Further, it is shown that the millisecond time constant depends on Cl- concentration, enabling the detection of the O intermediate. In the case of CO-myoglobin, spectral differences could be identified caused by mutations of the distal histidine of the heme binding pocket.

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