Proton magnetic resonance of the bovine spleen green heme‐protein

FEBS Letters

Inubushi, Toshiro¹  Ikeda-Saito, Masao¹ 

[1] Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6089, USA

关键词: Heme-protein;    Myeloperoxidase;    NMR;    (Bovine spleen);   

DOI  :  10.1016/0014-5793(87)80023-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ferric spleen green heme-protein exhibits hyperfine-shifted proton resonances between 90 and 20 ppm for the high-spin resting form and the chloride complex, and between 46 and −9.4 ppm for the low-spin nitrite complex. The proton NMR spectral profile of the enzyme is similar to that of lactoperoxidase, but different from those of common heme-proteins. The appearance of a resonance at 76 ppm in the ferrous enzyme shows the presence of a proximal histidine residue linked to the iron. The proton relaxation rates of bulk water indicate that chloride binds to the sixth position of the iron in the chloride complex of the enzyme.

【 授权许可】

Unknown