1H-NMR studies of high-potential iron-sulfur protein from the purple phototrophic bacterium, Rhodospirillum tenue
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1989.tb14696.x/fullpdf
Reference20 articles.
1. A high-potential nonheme iron protein (HiPIP)-linked, thiosulfate-oxidizing enzyme derived fromChromatium vinosum
2. Correlation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron transfer proteins.
3. Circular dichroism and redox properties of high redox potential ferredoxins
4. Hydrogen-1 nuclear magnetic resonance investigation of high-potential iron-sulfur proteins from Ectothiorhodospira halophila and Ectothiorhodospira vacuolata: a comparative study of hyperfine-shifted resonances
5. Primary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue.
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1. Reversible Super-Reduction of the Cubane [4Fe-4S](3+;2+;1+) in the High-Potential Iron-Sulfur Protein Under Non-Denaturing Conditions;European Journal of Biochemistry;2008-06-28
2. Electron-Nuclear Interactions;Encyclopedia of Magnetic Resonance;2007-03-15
3. Structure-Function Correlations in High-Potential IRON Proteins;Advances in Inorganic Chemistry;1998
4. Photoinduced Cyclic Electron Transfer in Rhodocyclus tenuis Cells: Participation of HiPIP or Cyt c8 Depending on the Ambient Redox Potential;Biochemistry;1997-10-01
5. 1H NMR of High-Potential Iron-Sulfur Protein from the Purple Non-Sulfur Bacterium Rhodoferax fermentans;European Journal of Biochemistry;1996-03
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