人类、恒河猴和牛碳酸酐酶中组氨酸的质子磁共振研究。

Proton magnetic resonance studies of histidines in human, rhesus monkey, and bovine carbonic anhydrases.

作者信息

Campbell I A, Lindskog S, White A I

出版信息

Biochim Biophys Acta. 1977 Oct 13;484(2):443-52. doi: 10.1016/0005-2744(77)90100-0.

PMID:20966

Abstract

Histidine C-2 proton resonances in rhesus monkey carbonic anhydrase B (carbonate hydro-lyase, EC 4.2.1.1) and bovine carbonic anhydrase were investigated using 270-MHz proton magnetic resonance. The results suggest that there are extensive three-dimensional homologies between the human B and rhesus B enzymes and between the human C and bovine enzymes. Resonances from solvent exchangeable protons have been observed in the 11-16 ppm range in the NMR spectra of human carbonic anhydrases B and C and bovine carbonic anhydrase. Up to five of these are sensitive to changes of pH and the presence of inhibitors. Three of these resonances are assigned to NH protons of the metal coordinated imidazole groups. These results are discussed in relation to various models for the catalytic mechanism of carbonic anhydrase.

摘要

使用270兆赫质子磁共振研究了恒河猴碳酸酐酶B（碳酸水解酶，EC 4.2.1.1）和牛碳酸酐酶中组氨酸C-2质子共振。结果表明，人B型和恒河猴B型酶之间以及人C型和牛型酶之间存在广泛的三维同源性。在人碳酸酐酶B和C以及牛碳酸酐酶的核磁共振谱中，已在11 - 16 ppm范围内观察到来自可与溶剂交换的质子的共振。其中多达五个对pH变化和抑制剂的存在敏感。这些共振中的三个被指定为金属配位咪唑基团的NH质子。结合碳酸酐酶催化机制的各种模型对这些结果进行了讨论。