Primary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. [35] Purification of (4Fe-4S)1—2− ferrodoxins (high-potential iron-sulfur proteins) from bacteria
2. The Complete Amino Acid Sequence of Chromatium High Potential Iron Sulfur Protein
3. Primary Structure of a High Potential Iron-Sulfur Protein from the Photosynthetic Bacterium Thiocapsa pfennigii
4. Primary structure of a high potential iron-sulfur protein from the purple non-sulfur photosynthetic bacterium Rhodopseudomonas gelatinosa.
5. Primary structure of a high potential iron sulfur protein from a moderately halophilic denitrifying coccus.
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1. High Potential Iron Sulfur Proteins;Encyclopedia of Inorganic and Bioinorganic Chemistry;2011-12-15
2. 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
3. High Potential Iron Sulfur Proteins;Handbook of Metalloproteins;2006-04-15
4. The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms;Microbiology;2005-05-01
5. HiPIP in Rubrivivax gelatinosus is firmly associated to the membrane in a conformation efficient for electron transfer towards the photosynthetic reaction centre;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2003-03
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