The Rubredoxin from Clostridium pasteurianum: Mutation of the Iron Cysteinyl Ligands to Serine. Crystal and Molecular Structures of Oxidized and Dithionite-Treated Forms of the Cys42Ser Mutant
- 17 April 1998
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (17), 4135-4150
- https://doi.org/10.1021/ja973162c
Abstract
No abstract availableThis publication has 64 references indexed in Scilit:
- X-ray absorption spectroscopy of Pyrococcus furiosus rubredoxinJBIC Journal of Biological Inorganic Chemistry, 1996
- Characterization of a Mutated Rubredoxin with a Cysteine Ligand of the Iron Replaced by SerineBiochemical and Biophysical Research Communications, 1995
- Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigasNature, 1995
- Zinc(II) coordination domain mutants of T4 gene 32 proteinBiochemistry, 1992
- Rubredoxin reductase of Pseudomonas oleovoransJournal of Molecular Biology, 1990
- NMR spectroscopy of cadmium-113(II) substituted gene 32 proteinBiochemistry, 1989
- Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filteringBiochemical and Biophysical Research Communications, 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Two-dimensional double quantum 1H NMR spectroscopy of proteinsBiochemical and Biophysical Research Communications, 1983
- Fluorescence X-ray absorption studies of rubredoxin and its model compoundsJournal of Molecular Biology, 1978