共 46 条
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.
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页码:240 / 246
页数:7
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