Nature of the Coupling between the High-Spin Fe(III) Heme and CuB(II) in the Active Site of Terminal Oxidases: Dual-Mode EPR Spectra of Fluoride Cytochrome bo3-Reference-Cited by-同舟云学术

Nature of the Coupling between the High-Spin Fe(III) Heme and CuB(II) in the Active Site of Terminal Oxidases: Dual-Mode EPR Spectra of Fluoride Cytochrome bo3

Published:1998-04-17 Issue:17 Volume:120 Page:4232-4233
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Oganesyan Vasily S.¹,Butler Clive S.¹,Watmough Nicholas J.¹,Greenwood Colin¹,Thomson Andrew J.¹,Cheesman Myles R.¹

Affiliation:

1. Centre for Metalloprotein Spectroscopy and Biology School of Chemical Sciences School of Biological Sciences University of East Anglia, Norwich NR4 7TJ, U.K.

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja974050o

Reference23 articles.

1. ENERGY TRANSDUCTION BY CYTOCHROME COMPLEXES IN MITOCHONDRIAL AND BACTERIAL RESPIRATION: The Enzymology of Coupling Electron Transfer Reactions to Transmembrane Proton Translocation

2. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

3. Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å

4. The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å

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