Incorporation of Transmembrane Peptides from the Vacuolar H+-ATPase in Phospholipid Membranes: Spin-Label Electron Paramagnetic Resonance and Polarized Infrared Spectroscopy-Reference-Cited by-同舟云学术

Incorporation of Transmembrane Peptides from the Vacuolar H+-ATPase in Phospholipid Membranes: Spin-Label Electron Paramagnetic Resonance and Polarized Infrared Spectroscopy

Published:2008-02-29 Issue:12 Volume:47 Page:3937-3949
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kóta Zoltán¹,Páli Tibor¹,Dixon Neil¹,Kee Terry P.¹,Harrison Michael A.¹,Findlay John B. C.¹,Finbow Malcolm E.¹,Marsh Derek¹

Affiliation:

1. Max-Planck-Institut für biophysikalische Chemie, Abt. Spektroskopie, 37070 Göttingen, Germany, Institute of Biophysics, Biological Research Centre, 6701 Szeged, Hungary, School of Chemistry and School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, U.K., and Department of Biological and Biomedical Sciences, Glasgow Caledonian University, Glasgow G4 0BA, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi7025112

Reference66 articles.

1. Proton translocation driven by ATP hydrolysis in V-ATPases

2. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology

3. Bafilomycin inhibits proton flow through the H+ channel of vacuolar proton pumps

4. Mutations in Subunit c of the Vacuolar ATPase Confer Resistance to Bafilomycin and Identify a Conserved Antibiotic Binding Site

5. Concanamycin A, the Specific Inhibitor of V-ATPases, Binds to the Vo Subunit c

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