1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate β proton
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(97)00995-2/fullpdf
Reference27 articles.
1. Keller R.M. Wüthrich K. Debrunner G. Proc. Natl. Acad. Sci. USA 69 1972 2073 2075
2. Structural studies of hemes and hemoproteins by nuclear magnetic resonance spectroscopy
3. La Mar G.N. de Ropp J.S. Berliner L. Reuben J. Biological Magnetic Resonance 12 1993 Plenum Press New York 1 78
4. Nuclear magnetic resonance of paramagnetic metalloproteins
5. The effect of cytochrome P-450cam on the NMR relaxation rate of water protons.
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