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Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy

Larsen, Randy W. and Li, Wei and Copeland, Robert A. and Witt, Stephan N. and Lou, Bih Show and Chan, Sunney I. and Ondrias, Mark R. (1990) Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy. Biochemistry, 29 (43). pp. 10135-10140. ISSN 0006-2960. https://resolver.caltech.edu/CaltechAUTHORS:20180212-143012991

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Abstract

Resonance Raman spectroscopy was employed to investigate the heme structures of catalytic intermediates of cytochrome c oxidase at room temperature. The high-frequency resonance Raman spectra were obtained for compound C (the two-electron-reduced dioxygen intermediate), ferryl (the three-electron-reduced dioxygen intermediate), and the fully oxidized enzyme. Compound C was formed by photolyzing CO mixed-valence enzyme in the presence of 02. The ferryl intermediate was formed by reoxidation of the fully reduced enzyme by an excess of H202. Two forms of the oxidized enzyme were prepared by reoxidizing the fully reduced enzyme with 02. Our data indicate that, in compound C, cyt a3 is either intermediate or low spin and is nonphotolabile and its oxidation state marker band, v4, appears at a higher frequency than that of the resting form of the enzyme. The ferryl intermediate also displays a low-spin cyt u3, which is nonphotolabile, and an even higher frequency for the oxidation state marker band, v4. The reoxidized form of cytochrome c oxidase with a Soret absorption maximum at 420 nm has an oxidation state marker band (u4) in a position similar to that of the resting form, while the spin-state region resembles that of compound C. This species subsequently decays to a second oxidized form of the enzyme, which displays a high-frequency resonance Raman spectrum identical with that of the original resting enzyme.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi00495a018DOIArticle
https://pubs.acs.org/doi/10.1021/bi00495a018PublisherArticle
ORCID:
AuthorORCID
Chan, Sunney I.0000-0002-5348-2723
Additional Information:© 1990 American Chemical Society. Received May 4, 1990; Revised Manuscript Received June 22, 1990. Research supported in part by Grants GM 22432 (to S.I.C.) and GM 33330 (to M.R.O.) from the National Institute of General Medical Sciences, US. Public Health Service, Grant RR 08139 (to M.R.O.) from the Division of Research Resources, National Institutes of Health, and the donors of the Petroleum Research Fund, administered by the American Chemical Society (to S.I.C.). Contribution No. 8103 from Division of Chemistry and Chemical Engineering, California Institute of Technology.
Funders:
Funding AgencyGrant Number
NIHGM 22432
NIHGM 33330
NIHRR 08139
American Chemical Society Petroleum Research FundUNSPECIFIED
Other Numbering System:
Other Numbering System NameOther Numbering System ID
Caltech Division of Chemistry and Chemical Engineering8103
Issue or Number:43
Record Number:CaltechAUTHORS:20180212-143012991
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20180212-143012991
Official Citation:Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy Randy W. Larsen, Wei Li, Robert A. Copeland, Stephan N. Witt, Bih Show Lou, Sunney I. Chan, and Mark R. Ondrias Biochemistry 1990 29 (43), 10135-10140 DOI: 10.1021/bi00495a018
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:84797
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:13 Feb 2018 21:07
Last Modified:03 Oct 2019 19:22

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