An investigation of Chromatium vinosum high-potential irondashsulfur protein by EPR and Mossbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions
- 20 September 1991
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1079 (3) , 253-262
- https://doi.org/10.1016/0167-4838(91)90066-9
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Amino acid sequence of high-redox-potential ferredoxin (HiPIP) isozymes from the extremely halophilic purple phototrophic bacterium, Ectothiorhodospira halophilaArchives of Biochemistry and Biophysics, 1985
- The bacteria of the sulphur cyclePhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1982
- A high-potential nonheme iron protein (HiPIP)-linked, thiosulfate-oxidizing enzyme derived fromChromatium vinosumCurrent Microbiology, 1979
- [20] Transition metal electron paramagnetic resonance related to proteinsPublished by Elsevier ,1978
- Magnetic studies of the four-iron high-potential, non-heme protein from Chromatium vinosumBiochimica et Biophysica Acta (BBA) - Protein Structure, 1975
- Mössbauer effect in the high-potential iron–sulphur protein from Chromatium. Evidence for the state of the iron atomsBiochemical Journal, 1974
- [62] High potential iron proteins: BacterialPublished by Elsevier ,1971
- Hyperfine structure of [57Fe]iron in the Mössbauer spectrum of the high-potential iron protein from ChromatiumBiochemical Journal, 1970
- Photosynthetic BacteriaAnnual Review of Microbiology, 1967
- Sudden freezing as a technique for the study of rapid reactionsBiochemical Journal, 1961