13C{13C} 2D NMR: A Novel Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates
- 9 March 2002
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 124 (13) , 3204-3205
- https://doi.org/10.1021/ja017733j
Abstract
Oxidized human [2Fe-2S] ferredoxin has a notably slow electronic relaxation rate, which precludes the observation of signals from nuclei near the iron−sulfur cluster by conventional 2D or 3D methods that utilize proton detection. We have demonstrated the utility of 13C{13C} CT-COSY in identifying connectivity information from fast relaxing carbon nuclei near the paramagnetic center, including those from residues that ligate the metal center.Keywords
This publication has 8 references indexed in Scilit:
- NMR Investigations of Clostridium pasteurianum Rubredoxin. Origin of Hyperfine 1H, 2H, 13C, and 15N NMR Chemical Shifts in Iron−Sulfur Proteins As Determined by Comparison of Experimental Data with Hybrid Density Functional CalculationsJournal of the American Chemical Society, 1998
- The solution structure of paramagnetic metalloproteinsProgress in Biophysics and Molecular Biology, 1996
- 1H AND 15N NMR Sequential Assignment, Secondary Structure, and Tertiary Fold of [2Fe-2S] Ferredoxin from Synechocystis sp. PCC 6803Biochemistry, 1995
- Protein Expression, Selective Isotopic Labeling, and Analysis of Hyperfine-Shifted NMR Signals of Anabaena 7120 Vegetative [2Fe-2S]FerredoxinArchives of Biochemistry and Biophysics, 1995
- Nuclear magnetic resonance of paramagnetic metalloproteinsChemical Reviews, 1993
- Are true scalar proton—proton connectivities ever measured in COSY spectra of paramagnetic macromolecules?Chemical Physics Letters, 1993
- 2D NMR assignment of hyperfine-shifted resonances in strongly paramagnetic metalloproteins: resting-state horseradish peroxidaseJournal of the American Chemical Society, 1991
- Identification of localized redox states in plant-type two-iron ferredoxins using the nuclear Overhauser effectBiochemistry, 1990