Structural control of the redox potentials and of the physiological activity by oligomerization of ferredoxin
- 1 May 1978
- journal article
- Published by Wiley in FEBS Letters
- Vol. 89 (1), 177-179
- https://doi.org/10.1016/0014-5793(78)80549-3
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Redox states of cytochrome c3 in the absence and presence of ferredoxinFEBS Letters, 1977
- Spectroscopic studies of the oxidation-reduction properties of three forms of ferredoxin from Desulphovibrio gigasBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- NMR characterization of three forms of ferredoxin from Desulphovibrio gigas, a sulphate reducerBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1977
- Purification, characterization and biological activity of three forms of ferredoxin from the sulfate-reducing bacterium Desulfovibrio gigasBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1976
- Physicochemical properties of flavodoxin from Desulfovibrio vulgarisBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
- A Comparison of Fe 4 S 4 Clusters in High-Potential Iron Protein and in FerredoxinProceedings of the National Academy of Sciences, 1972
- The Entatic StateCold Spring Harbor Symposia on Quantitative Biology, 1972
- Metalloenzymes: the entatic nature of their active sites.Proceedings of the National Academy of Sciences, 1968
- Dependance of sulfite reduction on a crystallized ferredoxin from Desulfovibrio gigasBiochemical and Biophysical Research Communications, 1966
- Cytochrome c3 and Desulphoviridin; Pigments of the Anaerobe Desulphovibrio desulphuricansJournal of General Microbiology, 1956