Interaction of soluble guanylate cyclase with YC-1: Kinetic and resonance Raman studies

被引:84
作者
Denninger, JW
Schelvis, JPM
Brandish, PE
Zhao, Y
Babcock, GT [1 ]
Marletta, MA
机构
[1] Michigan State Univ, Dept Chem, E Lansing, MI 48824 USA
[2] Michigan State Univ, LASER Lab, E Lansing, MI 48824 USA
[3] Univ Michigan, Sch Med, Howard Hughes Med Inst, Dept Biol Chem, Ann Arbor, MI 48109 USA
[4] Univ Michigan, Coll Pharm, Interdepartmental Program Med Chem, Ann Arbor, MI 48109 USA
关键词
D O I
10.1021/bi992332q
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The enzyme-soluble guanylate cyclase (sGC), which converts GTP to cGMP, is a receptor for the signaling agent nitric oxide (NO). YC-1, a synthetic benzylindazole derivative, has been shown to activate sGC in an NO-independent fashion. In the presence of carbon monoxide (CO), which by itself activates sGC approximately 5-fold, YC-1 activates sCC to a level comparable to stimulation by NO alone. We have used kinetic analyses and resonance Raman spectroscopy (RR) to investigate the interaction of YC-1 and CO with guanylate cyclase. In the presence of CO and 200 mu M YC-1, the V-max/K-m (GTP) increases 226-fold. While YC-1 does not perturb the RR spectrum of the ferrous form of baculovirus/Sf9 cell expressed sGC, it induces a shift in the Fe-CO stretching frequency for the GO-bound form from 474 to 492 cm(-1). Similarly, YC-1 has no effect on the RR spectrum of ferrous beta 1(1-385), the isolated sGC heme-binding domain, but shifts the nu(Fe-CO) of CO-beta 1(1-385) from 478 to 491 cm(-1), indicating that YC-1 binds in heme-binding region of sGC. In addition, the GO-bound forms of sGC and beta 1(1-385) in the presence of YC-1 lie on the nu(Fe-CO) vs nu(C-O) correlation curve for proximal ligands with imidazole character, which suggests that histidine remains the heme proximal ligand in the presence of YC-1. Interestingly, YC-1 does not shift nu(Fe-CO) for the CO-bound form of H105G(Im), the imidazole-rescued heme ligand mutant of beta 1(1-385). The data are consistent with binding of CO and YC-1 to the sGC hemebinding domain leading to conformational changes that give rise to an increase in catalytic turnover and a change in the electrostatic environment of the heme pocket.
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页码:4191 / 4198
页数:8
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