Non-equivalent natures of the coordinated imidazole rings of cytochromec3fromD. vulgarisMiyazaki F as studied by1H NMR
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)81289-X/fullpdf
Reference12 articles.
1. J.R. Postgate The Sulphate-reducing Bacteria 1984 Cambridge University Press Cambridge
2. Crystal structure and electron transfer properties of cytochrome c3.
3. Refined structure of cytochrome c3 at 1.8 Å resolution
4. Estimation of microscopic redox potentials of a tetraheme protein, cytochrome c3 of Desulfovibrio vulgaris, Miyazaki F and partial assignments of heme groups
5. Full assignment of heme redox potentials of cytochromec3ofD. vulgarisMiyazaki F by1H-NMR
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1. Role of π-Electron Systems in Stabilization of the Oxidized Tetraheme Architecture in Cytochromec3;Bulletin of the Chemical Society of Japan;2011-10-15
2. Strategic Roles of Axial Histidines in Structure Formation and Redox Regulation of Tetraheme Cytochrome c3;Biochemistry;2008-08-15
3. Identification of a Small Tetraheme Cytochrome c and a Flavocytochrome c as Two of the Principal Soluble Cytochromes c in Shewanella oneidensis Strain MR1;Applied and Environmental Microbiology;2001-07
4. Ionic Strength-Dependent Physicochemical Factors in Cytochrome c3 Regulating the Electron Transfer Rate;Biophysical Journal;1998-09
5. Nmr Study Of Active Sites In Paramagnetic Haemoproteins;Annual Reports on NMR Spectroscopy;1998
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