Connectivity of proton and carbon spectra of the blue copper protein, plastocyanin, established by two‐dimensional nuclear magnetic resonance
1983; Wiley; Volume: 162; Issue: 1 Linguagem: Inglês
10.1016/0014-5793(83)81047-3
ISSN1873-3468
AutoresChristopher L. Kojiro, John L. Markley,
Tópico(s)Spectroscopy and Quantum Chemical Studies
ResumoNMR studies of plastocyanin have centered on the ligands to the copper atom at the active site, particularly histidines‐37 and ‐87. Heteronuclear ( 13 C, 1 H) J ‐connectivity spectroscopy has enabled cross assignment of 1 H and 13 C NMR resonances from the two copper‐ligated histidines. In addition to providing assignments of the 13 C resonances, the two‐dimensional Fourier transform NMR results require the reversal of the original 1 H NMR assignments to the ring protons of histidine‐37. The line widths of the ring protons of histidine‐87 are field‐dependent leading to determination of the reduced lifetime of the proton on the N δ atom (about 400 μs).
Referência(s)