Renal mitochondrial ferredoxin active in 25-hydroxyvitamin D3 1.alpha.-hydroxylase. Characterization of the iron-sulfur cluster using interprotein cluster transfer and electron paramagnetic resonance spectroscopy
- 1 May 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (10) , 2172-2176
- https://doi.org/10.1021/bi00551a027
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Purification and properties of chick renal mitochondrial ferredoxinBiochemistry, 1980
- Characterization of the iron-sulfur centers in succinate dehydrogenase.Proceedings of the National Academy of Sciences, 1979
- Synthetic analogs of the active sites of iron-sulfur proteins. 15. Comparative polarographic potentials of the [Fe4S4(SR)4]2-,3- and Clostridium pasteurianum ferredoxin redox couplesJournal of the American Chemical Society, 1977
- Quantitative extrusions of the iron sulfide(Fe4S4*) cores of the active sites of ferredoxins and the hydrogenase of Clostridium pasteurianumJournal of the American Chemical Society, 1977
- Isolation of chick renal mitochondrial ferredoxin active in the 25-hydroxyvitamin D3-1alpha-hydroxylase system.Journal of Biological Chemistry, 1976
- [90] Isolation of cytochromes P-450 and P-420Published by Elsevier ,1967
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTIONJournal of Biological Chemistry, 1949