Structural characterization of nitric oxide-bound soluble Guanylate Cyclase using resonance Raman spectroscopy

被引:1
作者
Pal, Biswajit [1 ]
Tanaka, Katsuhiro [2 ]
Takenaka, Shigeo [2 ]
Shaik, Tajith B. [1 ]
Kitagawa, Teizo [3 ]
机构
[1] CSIR, Ctr Cellular & Mol Biol, Hyderabad 500007, Andhra Pradesh, India
[2] Osaka Prefecture Univ, Dept Vet Sci, Sakai, Osaka 5938531, Japan
[3] Univ Hyogo, Grad Sch Life Sci, Picobiol Inst, Kamigori, Hyogo 6781297, Japan
关键词
soluble Guanylate Cyclase; resonance Raman spectroscopy; GTP; YC-1; BAY; nitric oxide; ACTIVATION; HEME; BINDING; NO; MYOGLOBIN; YC-1; IDENTIFICATION; MECHANISM; RESIDUES; DEUTERATION;
D O I
10.1142/S1088424613500375
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Mammalian soluble Guanylate Cyclase (sGC), working as a physiological NO receptor, is investigated using resonance Raman spectroscopy for NO bound states with different saturation levels in the presence and absence of effectors. The Fe-NO (nu(Fe-NO)) and N-O (nu(N-O)) stretching bands appeared at 521 and 1681 cm(-1), respectively, without effectors, but nu(N-O) was split into 1681 and 1699 cm(-1) in the presence of GTP and shifted to 1687 cm(-1) in the presence of YC-1 or BAY 41-2272, while nu(Fe-NO) remained unaltered. The split two nu(N-O) bands were independent of NO saturation levels. GTP or YC-1/BAY 41-2272 altered the vinyl and propionate bending modes from 423 to 399 cm(-1) and 376 to 367 cm(-1), respectively. Based on these observations, allosteric effects on NO ... protein interactions are discussed.
引用
收藏
页码:240 / 246
页数:7
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