Connectivity of proton and carbon spectra of the blue copper protein, plastocyanin, established by two‐dimensional nuclear magnetic resonance

FEBS Letters

Kojiro, Christopher L.¹  Markley, John L.¹ 

[1] Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA

关键词: 2DFT-NMR;    Plastocyanin;    Electron transport;    Photosynthesis;    Histidine;    Cu-ligand;    2DFT-NMR;    two-dimensional Fourier-transform nuclear magnetic resonance;    TSP;    sodium 3-(trimethylsilyl) propionic acid;    TMS;    tetramethylsilane;    ppm;    parts per million;   

DOI  :  10.1016/0014-5793(83)81047-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

NMR studies of plastocyanin have centered on the ligands to the copper atom at the active site, particularly histidines-37 and -87. Heteronuclear (¹³C, ¹H) J-connectivity spectroscopy has enabled cross assignment of ¹H and ¹³C NMR resonances from the two copper-ligated histidines. In addition to providing assignments of the ¹³C resonances, the two-dimensional Fourier transform NMR results require the reversal of the original ¹H 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).

【 授权许可】

Unknown