Abstract
The 8Fe-8S ferredoxin from Clostridium pasteurianum was investigated by 1D and 2D 1H NMR. Spectra of a well-structured, full native preparation of the oxidized protein in 1 M NaCl at pH 8.0 are presented. Assignments of non-isotropically shifted resonances in the diamagnetic region of the spectrum, namely those of the unique aromatic residues F30 and Y2, are presented for the first time.
| Original language | English |
|---|---|
| Pages (from-to) | 577-585 |
| Number of pages | 9 |
| Journal | Biochemistry International |
| Volume | 26 |
| Issue number | 4 |
| Publication status | Published - 20 Jan 1992 |
Keywords
- ferredoxin
- phenylalanine
- tyrosine
- article
- Clostridium pasteurianum
- nonhuman
- priority journal
- protein structure
- proton nuclear magnetic resonance