Share Email Print

Proceedings Paper

Fourier Transform Infrared And Resonance Raman Characterization Of Cytochrome Ba[sub]3[/sub] From Thermus Thermophilus
Author(s): Olof Einarsdottir; R. Brian Dyer; Patrick M. Killough; James A. Fee; William H. Woodruff
Format Member Price Non-Member Price
PDF $17.00 $21.00

Paper Abstract

Resonance Raman and Fourier transform infrared spectra of several derivatives of cytochrome ba3, a newly discovered terminal oxidase of the bacterium Thermus thermophilus, are reported. The RR features characteristic of cytochrome a3 are uniquely observed without interference from cytochrome b by subtraction of the analogous cytochrome b5 spectra. The spin state indicator peaks of the a3 heme appear at unusually high frequencies, suggesting a uniquely small heme core size. Multiple C-0 and Fe-N(Im) peaks are observed in the FTIR and RR spectra, respectively. Their relative intensities are temperature-dependent suggesting the presence of discrete interconverting conformers of the enzyme. Thermodynamic parameters for interconversion of these conformers are derived. The C-0 infrared stretching frequencies of the fully reduced carbon-monoxy enzyme show that CO binds to Cue following photodissociation of CO from the heme a3 at all temperatures up to ambient.

Paper Details

Date Published: 5 July 1989
PDF: 9 pages
Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); doi: 10.1117/12.951596
Show Author Affiliations
Olof Einarsdottir, University of California (United States)
R. Brian Dyer, University of California (United States)
Patrick M. Killough, University of California (United States)
James A. Fee, University of California (United States)
William H. Woodruff, University of California (United States)

Published in SPIE Proceedings Vol. 1055:
Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology
Fran Adar; James E. Griffiths; Jeremy M. Lerner, Editor(s)

© SPIE. Terms of Use
Back to Top