Proton magnetic resonance studies of 7 Fe ferredoxins
Open Access
- 25 July 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 158 (2), 208-212
- https://doi.org/10.1016/0014-5793(83)80579-1
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Isolation and characterization of a ferredoxin from Mycobacterium smegmatis takeoBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Mössbauer spectroscopic evidence for the conversion of [4 Fe—4 S] clusters in Bacillus stearothermophilus ferredoxin into [3 Fe—3 S] clustersFEBS Letters, 1982
- Resonance Raman and electron paramagnetic resonance studies on oxidized and ferricyanide-treated Clostridium pasteurianum ferredoxin. Vibrational assignments from 34S shifts and evidence for conversion of 4 to 3 iron-sulfur clusters via oxidative damage. Vibrational assignments from 34S shifts and evidence for conversion of 4 to 3 iron-sulfur clusters via oxidative damage.Journal of Biological Chemistry, 1982
- Proton magnetic resonance studies of Azotobacter vinelandii ferredoxin I. Evidence for a difference in coordination of the 3Fe centers in azotobacter vinelandii ferredoxin I and desulfovibrio gigas ferredoxin II.Journal of Biological Chemistry, 1981
- Purification, some properties and amino acid sequence of Thermus Thermophilus HB8 ferredoxinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- Mycobacterium smegmatis ferredoxin: A unique distribution of cysteine residues constructing iron—sulfur clustersFEBS Letters, 1979
- Pseudomonas ovalis ferredoxin: similarity to Azotobacter and Chromatium ferredoxinsFEBS Letters, 1978
- Properties of iron-sulfur protein isolated from pseudomonasovalisBiochemical and Biophysical Research Communications, 1976
- High and low reduction potential 4Fe-4S clusters in Azotobacter vinelandii (4Fe-4S) 2ferredoxin I. Influence of the polypeptide on the reduction potentials.Journal of Biological Chemistry, 1975
- A Comparison of Fe 4 S 4 Clusters in High-Potential Iron Protein and in FerredoxinProceedings of the National Academy of Sciences, 1972