Entry of water into the distal heme pocket of soluble guanylate cyclase beta 1 H-NOX domain alters the ligated CO structure: a resonance Raman and in silico simulation study

doi:10.1039/c6ra06515e

	Entry of water into the distal heme pocket of soluble guanylate cyclase beta 1 H-NOX domain alters the ligated CO structure: a resonance Raman and in silico simulation study
	Zhang, Yuebin 2,3; Chen, Lei 2,4; Xu, Haoran 2; Li, Yan 3; Li, Chen 1; Liu, Li 2; Ogura, Takashi 1; Kitagawa, Teizo 1; Li, Zhengqiang 2
刊名	RSC ADVANCES
	2016
卷号	6 期号:49 页码:43707-43714
ISSN号	2046-2069
DOI	10.1039/c6ra06515e
文献子类	Article
英文摘要	Resonance Raman spectra (rRS) of the CO-Ns H-NOX (heme nitric oxide and oxygen binding) complex, a bacterial model for the mammalian CO-sGC (soluble Guanylyl Cyclase) complex, are reported. The CO-Ns H-NOX complex exhibited two Fe-CO stretching modes (nu(Fe-CO)) with an intense band at 470 cm(-1) and a weaker band at 494 cm(-1), which are very similar to those observed for a CO-ligated full-length bovine lung sGC. However, the rRS of truncated sGC beta 1((1-194)) H-NOX exhibited comparable bands, but with a reversed intensity ratio, the nu(Fe-CO) at 492 cm(-1) was dominant. This difference is similar to that observed for six-coordinate CO-sGC's in the absence and presence of YC-1, an effector. Molecular dynamic (MD) simulations of truncated sGC beta 1((1-194)) H-NOX demonstrate that water may enter the distal heme pocket to form a hydrogen bond with ligated CO; whereas it hardly happens to Ns H-NOX. By employing density functional theory (DFT) analysis, we calculated the C-O and Fe-CO stretching frequencies of the isolated imidazole (ImH)(-) and porphyrin (P) containing complex, (ImH) FeP(CO), in the presence or absence of water molecules. The calculated rRS exhibited bands at a higher nu(Fe-CO) frequency in the presence of water, in agreement with observations for truncated sGC, further supporting the hypothesis that water access to the distal heme pocket influences the ligation of CO, although the proximal effects remain to be elucidated.
WOS关键词	MOLECULAR-DYNAMICS METHOD ; NITRIC-OXIDE ; CARBON-MONOXIDE ; SYNERGISTIC ACTIVATION ; BINDING ; PROTEINS ; HEMOGLOBIN ; VIBRATIONS ; MECHANISM ; MODELS
WOS研究方向	Chemistry
语种	英语
出版者	ROYAL SOC CHEMISTRY
WOS记录号	WOS:000375611100108
内容类型	期刊论文
源URL	[http://cas-ir.dicp.ac.cn/handle/321008/170916]
专题	大连化学物理研究所_中国科学院大连化学物理研究所
通讯作者	Kitagawa, Teizo; Li, Zhengqiang
作者单位	1.Univ Hyogo, RSC UH Leading Program Ctr, Grad Sch Life Sci, Picobiol Inst, 1-1-1 Koto, Sayo, Hyogo 6795148, Japan 2.Jilin Univ, Sch Life Sci, Key Lab Mol Enzymol & Engn, Minist Educ, Changchun 130012, Peoples R China 3.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Mol React Dynam, Dalian 116023, Peoples R China 4.Jilin Univ, Inst Atom & Mol Phys, Changchun 130012, Peoples R China
推荐引用方式 GB/T 7714	Zhang, Yuebin,Chen, Lei,Xu, Haoran,et al. Entry of water into the distal heme pocket of soluble guanylate cyclase beta 1 H-NOX domain alters the ligated CO structure: a resonance Raman and in silico simulation study[J]. RSC ADVANCES,2016,6(49):43707-43714.
APA	Zhang, Yuebin.,Chen, Lei.,Xu, Haoran.,Li, Yan.,Li, Chen.,...&Li, Zhengqiang.(2016).Entry of water into the distal heme pocket of soluble guanylate cyclase beta 1 H-NOX domain alters the ligated CO structure: a resonance Raman and in silico simulation study.RSC ADVANCES,6(49),43707-43714.
MLA	Zhang, Yuebin,et al."Entry of water into the distal heme pocket of soluble guanylate cyclase beta 1 H-NOX domain alters the ligated CO structure: a resonance Raman and in silico simulation study".RSC ADVANCES 6.49(2016):43707-43714.