A 1 H NMR study of bovine cytochrome oxidase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(89)81809-5/fullpdf
Reference29 articles.
1. Pumping of protons from the mitochondrial matrix by cytochrome oxidase
2. Cytochrome c oxidase is three-copper, two-heme-A protein
3. Studies of the heme components of cytochrome c oxidase by EPR spectroscopy
4. The Structure of the Cytochrome a3-cuB Site of Mammalian Cytochrome c Oxidase as probed by MCD and EPR Spectroscopy
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1. Proton NMR study of the heme environment in bacterial quinol oxidases;Archives of Biochemistry and Biophysics;2004-01
2. NMR Studies of Paramagnetic Systems to Characterise Small Molecule:Protein and Protein:Protein Interactions;Nuclear Magnetic Resonance of Paramagnetic Macromolecules;1995
3. Nuclear magnetic resonance of paramagnetic metalloproteins;Chemical Reviews;1993-12
4. A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex;European Journal of Biochemistry;1992-09
5. 1H NMR determination of the ionization constant of a carboxylic acid group of a haem protein in mixed aqueous-organic solvents using the super WEFT sequence;Magnetic Resonance in Chemistry;1991-10
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