𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Paramagnetic 1H NMR saturation transfer study of ligand exchange in iron(III) myoglobins

✍ Scribed by Yasuhiko Yamamoto; Yoshio Inoue; Tomohiko Suzuki


Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
811 KB
Volume
31
Category
Article
ISSN
0749-1581

No coin nor oath required. For personal study only.

✦ Synopsis


Abstract

^1^H NMR saturation transfer experiments were successfully used in connecting iron(III) high‐ and low‐spin forms of equine, the mollusc Dolabella auricularia and the shark Mustelus japonicus myoglobins. With the known signal assignments in the high‐spin form, a haem peripheral proton resonances in met‐azido and met‐imidazole complexes of the myoglobins have been straightforwardly assigned via the saturation transfer connectivities. Analysis of the extent of the saturation transfer provided the kinetics of the ligand exchange.


📜 SIMILAR VOLUMES


Comparative 1H NMR studies of saturation
✍ Koji Nakamura; Masaru Sogami; Seiichi Era; Shigeru Matsushima; Yasutomi Kinosada 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 182 KB

## Abstract Saturation transfer in cross‐linked copolymer gels and excised intact and perforating trauma‐induced cataract mouse lenses (4‐ or 8‐week‐old) were studied using intermolecular cross‐relaxation rates (1/__T__~IS~(H~2~O); 1/__T__~IS~), monitored with __f__~2~‐irradiation at −8.79, −4.00,

Two-dimensional 1H NMR studies of Ca(II)
✍ Li-june Ming 📂 Article 📅 1993 🏛 John Wiley and Sons 🌐 English ⚖ 581 KB

## Abstract Substitution of Yb^3+^ for the Ca^2+^ in bovine α‐lactalbumin affords a derivative that gives rise to several isotropically shifted ^1^H NMR signals in the range 80 to − 35 ppm in D~2~O. Despite the broadness of the isotropically shifted features, cross signals in both NOESY and COSY sp