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Proceedings Paper

Nanosecond time-resolved natural and magnetic circular dichroism spectroscopy of protein dynamics
Author(s): Robert A. Goldbeck; Sophie Bjorling; David S. Kliger
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Paper Abstract

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.

Paper Details

Date Published: 1 June 1991
PDF: 14 pages
Proc. SPIE 1432, Biomolecular Spectroscopy II, (1 June 1991); doi: 10.1117/12.44205
Show Author Affiliations
Robert A. Goldbeck, Univ. of California/Santa Cruz (United States)
Sophie Bjorling, Univ. of California/Santa Cruz (United States)
David S. Kliger, Univ. of California/Santa Cruz (United States)

Published in SPIE Proceedings Vol. 1432:
Biomolecular Spectroscopy II
Robert R. Birge; Laurence A. Nafie, Editor(s)

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