The dicyclohexylcarbodiimide-binding protein of the mitochondrial ATPase complex from beef heart
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(78)80941-7/fullpdf
Reference22 articles.
1. Dicyclohexylcarbodiimide — An inhibitor of oxidative phosphorylation
2. A comparison of the effects of NN′-dicyclohexylcarbodi-imide, oligomycin A and aurovertin on energy-linked reactions in mitochondria and submitochondrial particles
3. The identification of the site of action of NN′-dicyclohexylcarbodi-imide as a proteolipid in mitochondrial membranes
4. Identification of the dicyclohexylcarbodiimide-binding protein in the oligomycin-sensitive adenosine triphosphatase from bovine heart mitochondria
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1. Two Distinct Proton Binding Sites in the ATP Synthase Family;Biochemistry;2007-10-01
2. A Study of the Dicyclohexylcarbodiimide-Binding Component of the Mitochondrial ATPase Complex from Beef Heart;European Journal of Biochemistry;2005-03-03
3. The KdpF Subunit Is Part of the K+-translocating Kdp Complex of Escherichia coli and Is Responsible for Stabilization of the Complex in Vitro;Journal of Biological Chemistry;1999-12
4. Proton-Translocating Carboxyl of Subunit c of F1Fo H+-ATP Synthase: The Unique Environment Suggested by the pKa Determined by 1H NMR;Biochemistry;1995-12
5. ATP synthase subunit c storage in the polymorphonucleocytes of late infantile and juvenile batten patients;International Journal of Developmental Neuroscience;1995-08
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