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- W2066755897 abstract "The oxidized forms of the redox proteins putidaredoxin and putidaredoxin-15N were prepared by insertion of suitable plasmids into E. coli and the structures of the proteins were studied by homo- and heteronuclear 1H and 15N NMR methods, including identification of 15N resonance types by one- and two-dimensional DEPT spectrum editing and measurements of 15N chemical shifts, coupling constants, nuclear Overhauser effects and spin–lattice relaxation times. Direct detection of 15N NMR spectra revealed a number of 15N resonances that have not been found in previous 1H detected NMR studies. These resonances include a set of 16 paramagnetically broadened signals from 15N nuclei that are structurally close to the iron–sulfur cluster of the protein, proline backbone 15N resonances and 15N signals from the side-chains of glutamine and lysine residues. Reduced distances between certain paramagnetically affected 15N nuclei and the center of the iron–sulfur cluster were calculated from the 15N spin–lattice relaxation times, based on the assumption of a dominant electron–nuclear dipole–dipole relaxation mechanism. Ranked by size, these distances agree with those computed from coordinates of a published structure of putidaredoxin determined by 1H NMR and analogy with an Anabaena ferredoxin. © 1997 John Wiley & Sons, Ltd." @default.
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- W2066755897 date "1997-11-01" @default.
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- W2066755897 title "Investigation of the paramagnetic domain of putidaredoxin by nitrogen-15 NMR spectroscopy" @default.
- W2066755897 doi "https://doi.org/10.1002/(sici)1097-458x(199711)35:11<743::aid-omr166>3.0.co;2-w" @default.
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