Direct Observation of Redox-Linked Histidine Protonation Changes in the Iron−Sulfur Protein of the Cytochrome bc1 Complex by ATR-FTIR Spectroscopy-Reference-Cited by-同舟云学术

Direct Observation of Redox-Linked Histidine Protonation Changes in the Iron−Sulfur Protein of the Cytochrome bc1 Complex by ATR-FTIR Spectroscopy

Published:2005-02-18 Issue:11 Volume:44 Page:4230-4237
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Iwaki Masayo¹,Yakovlev Gregory¹,Hirst Judy¹,Osyczka Artur¹,Dutton P. Leslie¹,Marshall Douglas¹,Rich Peter R.¹

Affiliation:

1. Glynn Laboratory of Bioenergetics, Department of Biology, University College London, Gower Street, London WC1E 6BT, U.K., Medical Research Council Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, U.K., and The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, 1004 Stellar-Chance Building, 422 Curie Boulevard, Philadelphia, Pennsylvania 19104

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi047533v

Reference71 articles.

1. Zhang, Z., Huang, L., Shulmeister, V. M., Chi, Y.I., Kim, K. K., Hung, L.W., Crofts, A. R., Berry, E. A., and Kim, S.H. (1998) Electron transfer by domain movement in cytochromebc1,Nature392, 677−684.

2. Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex

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