Fourier Transform Infrared And Resonance Raman Characterization Of Cytochrome Ba[sub]3[/sub] From Thermus Thermophilus

Olof Einarsdottir; R. Brian Dyer; Patrick M. Killough; James A. Fee; William H. Woodruff

doi:10.1117/12.951596

5 July 1989 Fourier Transform Infrared And Resonance Raman Characterization Of Cytochrome Ba₃ From Thermus Thermophilus

Olof Einarsdottir, R. Brian Dyer, Patrick M. Killough, James A. Fee, William H. Woodruff

Proceedings Volume 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology; (1989) https://doi.org/10.1117/12.951596
Event: OE/LASE '89, 1989, Los Angeles, CA, United States

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.

Citation Download Citation

Olof Einarsdottir, R. Brian Dyer, Patrick M. Killough, James A. Fee, and William H. Woodruff "Fourier Transform Infrared And Resonance Raman Characterization Of Cytochrome Ba₃ From Thermus Thermophilus", Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); https://doi.org/10.1117/12.951596

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