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1 June 1991 Nanosecond time-resolved natural and magnetic circular dichroism spectroscopy of protein dynamics
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Proceedings Volume 1432, Biomolecular Spectroscopy II; (1991)
Event: Optics, Electro-Optics, and Laser Applications in Science and Engineering, 1991, Los Angeles, CA, United States
A recently developed ellipsometric technique for the nanosecond time-resolved measurement of natural and magnetic circular dichroism (TRCD and TRMCD) spectra is discussed and applications to dynamical studies of biologically important molecules, principally hemeproteins, are presented. Nanosecond TRCD spectra of the Soret band of hemoglobin and myoglobin have been measured after photolysis of the carbonmonoxy complex. The TRCD of the photoreduction of metmyoglobin has also been studied. Nanosecond TRMCD spectroscopy of cytochrome c oxidase (cytochrome aa3) gives information about the spin state of the iron in the heme a3 transient intermediate formed after photolysis of the CO complex. Applications of TRMCD spectroscopy to cytochromes ba3 and c3 are also discussed, as are TRCD studies of phytochrome proteins. Recent progress in characterizing and eliminating spectral artifacts arising from photoselection in photolyzed proteins is summarized.
© (1991) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Robert A. Goldbeck, Sophie Bjorling, and David S. Kliger "Nanosecond time-resolved natural and magnetic circular dichroism spectroscopy of protein dynamics", Proc. SPIE 1432, Biomolecular Spectroscopy II, (1 June 1991);

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