Assignment of hyperfine-shifted heme carbon resonances in ferricytochromeb5
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00500-9/fullpdf
Reference27 articles.
1. Mechanism of interaction between cytochromes P-450 RLM5 and b5: Evidence for an electrostatic mechanism involving cytochrome b5 heme propionate groups
2. Cytochrome b5 from a Normal Human Liver
3. Catalysis of Methemoglobin Reduction
4. The electronic g-tensor in cytochrome b5: High resolution proton magnetic resonance studies
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1. Hemoglobina extracelular gigante de Glossoscolex paulistus: um extraordinário sistema supramolecular hemoproteico;Química Nova;2011
2. Recent developments in the 13 C NMR spectroscopic analysis of paramagnetic hemes and heme proteins;Analytical and Bioanalytical Chemistry;2004-03-01
3. Complete isomer-specific 1H and 13C NMR assignments of the heme resonances of rat liver outer mitochondrial membrane cytochrome b 5;JBIC Journal of Biological Inorganic Chemistry;1999-02
4. and NMR studies of a truncated heme domain from Chlorella vulgaris nitrate reductase: signal assignment of the heme moiety;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1998-01
5. Paramagnetic NMR shifts in cyanoferricytochrome c;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1997-09
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