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Resonance Raman Spectra of Cytochrome c Oxidase. Excitation in the 600-nm Region

Bocian, David F. and Lemley, Ann T. and Petersen, Nils O. and Brudvig, Gary W. and Chan, Sunney I. (1979) Resonance Raman Spectra of Cytochrome c Oxidase. Excitation in the 600-nm Region. Biochemistry, 18 (20). pp. 4396-4402. ISSN 0006-2960. http://resolver.caltech.edu/CaltechAUTHORS:20160815-122514293

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Abstract

The resonance Raman (RR) spectra of oxidized, reduced, and oxidized cyanide-bound cytochrome c oxidase with excitation at several wavelengths in the 600-nm region are presented. No evidence is found for laser-induced photoreduction of the oxidized protein with irradiation at λ ~600 nm at 195 K, in contrast to the predominance of this process upon irradiation in the Soret region at this temperature. The Raman spectra of all three protein species are very similar, and there are no Raman bands which are readily assignable to either cytochrome a or cytochrome a3, exclusively. The Raman spectra of the three protein species do, however, exhibit a number of bands not observed in the RR spectra of other hemoproteins upon excitation in their visible absorption bands. In particular, strong Raman bands are observed in the lowf-requency region of the RR spectra ( <500 cm^-1). The frequencies of these bands are similar to those of the copper-ligand vibrations observed in the RR spectra of type 1 copper proteins upon excitation in the 600-nm absorption band characteristic of these proteins. In cytochrome c oxidase, these bands do not disappear upon reduction of the protein and, therefore, cannot be attributed to copper-ligand vibrations. Thus, all the observed RR bands are associated with the two heme A moieties in the enzyme.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi00587a020DOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi00587a020PublisherArticle
ORCID:
AuthorORCID
Chan, Sunney I.0000-0002-5348-2723
Additional Information:© 1979 American Chemical Society. Received December 1, 1978. Contribution No. 5906 from the Arthur Amos Noyes Laboratory of Chemical Physics (D.F.B., G. W.B., and S.J.C.)D.F.B., G.W.B., and S.I.C. were supported by Grant GM22432 from the National Institute of General Medical Sciences, U.S. Public Health Service, and by BRSG Grant RR07003 awarded by the Biomedical Research Support Grant Program, Division of Research Resources, National Institutes of Health. G.W.B. is a recipient of a National Institutes of Health predoctoral traineeship. A.T.L. was supported by Grant EY01377 awarded to Aaron Lewis by the National Eye Institute, U.S. Public Health Service. The resonance Raman studies reported here were undertaken in the laboratory of Professor Aaron Lewis, whom we gratefully acknowledge. The authors also thank William Lambert for aiding in the studies of laser-induced photo reduction and Professor Ahmed Zewail for the use of the facilities in his laboratory.
Funders:
Funding AgencyGrant Number
National Institute of General Medical SciencesGM22432
NIHRR07003
NIH Predoctoral FellowshipUNSPECIFIED
National Eye InstituteEY01377
Other Numbering System:
Other Numbering System NameOther Numbering System ID
Arthur Amos Noyes Laboratory of Chemical Physics5906
Record Number:CaltechAUTHORS:20160815-122514293
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20160815-122514293
Official Citation:Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600-nm region David F. Bocian, Ann T. Lemley, Nils O. Petersen, Gary W. Brudvig, and Sunney I. Chan Biochemistry 1979 18 (20), 4396-4402 DOI: 10.1021/bi00587a020
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:69623
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:15 Aug 2016 22:02
Last Modified:15 Aug 2016 22:02

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