Resonance Raman characterization of soluble guanylate cyclase expressed from baculovirus.
Resonance Raman characterization of soluble guanylate cyclase expressed from baculovirus.
复制标题
DOI：
10.1021/bi971934b
复制
发表时间：
1998-02
期刊：
影响因子：
2.9
通讯作者：
B. Fan;G. Gupta;R. Danziger;J. Friedman;D. Rousseau
中科院分区：
文献类型：
--
作者：
B. Fan;G. Gupta;R. Danziger;J. Friedman;D. Rousseau
Resonance Raman spectra of the alpha 1 beta 1 isoform of bovine lung soluble guanylate cyclase expressed from baculovirus have been measured. The spectra show that the ferric heme is five-coordinate high spin whereas the ferrous heme in the absence of added exogenous ligands is a mixture of six-coordinate low spin and five-coordinate high spin. In the Fe-CO-derivative, the correlation between the Fe-CO frequency (497 cm-1) and the C-O frequency (1959 cm-1) demonstrates that the proximal ligand in our preparation is histidine. The Fe-NO stretching frequency (found at 520 cm-1) and other spectral features of the ferrous Fe-NO-bound sGC are similar to those reported by Deinum et al. (1) and Yu et al. (2). These data indicate that although large preparation-dependent differences in the occupancy of the distal pocket exist, all the preparations have the same proximal histidine ligation and share the same mechanism of activation by NO.
