The Solution Structure Refinement of the Paramagnetic Reduced High-Potential Iron-Sulfur Protein I from Ectothiorhodospira Halophila by Using Stable Isotope Labeling and Nuclear Relaxation-Reference-Cited by-同舟云学术

The Solution Structure Refinement of the Paramagnetic Reduced High-Potential Iron-Sulfur Protein I from Ectothiorhodospira Halophila by Using Stable Isotope Labeling and Nuclear Relaxation

Published:1996-10 Issue:2 Volume:241 Page:440-452
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

Bertini Ivano,Couture Manon M. J.,Donaire Antonio,Eltis Lindsay D.,Felli Isabella C.,Luchinat Claudio,Piccioli Mario,Rosato Antonio

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1996.00440.x/fullpdf

Reference47 articles.

1. The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance

2. Three-Dimensional Solution Structure of the Cyanide Adduct of a Variant of Saccharomyces cerevisiae Iso-1-cytochrome c Containing the Met80Ala Mutation. Identification of Ligand-Residue Interactions in the Distal Heme Cavity

3. The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR

4. Three-Dimensional Solution Structure of the Oxidized High Potential Iron-Sulfur Protein from Chromatium vinosum through NMR. Comparative Analysis with the Solution Structure of the Reduced Species

5. The Solution Structure of Oxidized HiPIP I fromEctothiorhodospira halophila; Can NMR Spectroscopy Be Used to Probe Rearrangements Associated with Electron Transfer Processes?

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