Asymmetric Binding of the High-Affinity QH•- Ubisemiquinone in Quinol Oxidase (bo3) from Escherichia coli Studied by Multifrequency Electron Paramagnetic Resonance Spectroscopy-Reference-Cited by-同舟云学术

Asymmetric Binding of the High-Affinity QH•- Ubisemiquinone in Quinol Oxidase (bo3) from Escherichia coli Studied by Multifrequency Electron Paramagnetic Resonance Spectroscopy

Published:2003-04-24 Issue:19 Volume:42 Page:5632-5639
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Grimaldi S.¹,Ostermann T.¹,Weiden N.¹,Mogi T.¹,Miyoshi H.¹,Ludwig B.¹,Michel H.¹,Prisner T. F.¹,MacMillan F.¹

Affiliation:

1. Institut für Physikalische und Theoretische Chemie and Institut für Biochemie, J. W. Goethe Universität Frankfurt, D-60439 Frankfurt am Main, Germany, Max-Planck Institut für Biophysik, D-60528 Frankfurt am Main, Germany, Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, ATP System Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation (JST), Nagatsuta, Midori-ku, Yokohama 226-0026,...

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi034010z

Reference53 articles.

1. Shinkarev, M. Y., and Wraight, C. A. (1993) inThe Photosynthetic Reaction Center(Deisenhofer, J., and Norris, J. R. Eds.) Vol. 1, pp 194−255, Academic Press, San Diego.

2. The primary and secondary acceptors in bacterial photosynthesis III. Characterization of the quinone radicals Q A − ⋅ and Q B − ⋅ by EPR and ENDOR

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