2009 Fiscal Year Final Research Report

Signal discrimination analyses based on the domain structure of soluble guanylate cyclase

Research Project

Project/Area Number	19510224
Research Category	Grant-in-Aid for Scientific Research (C)
Allocation Type	Single-year Grants
Section	一般
Research Field	Living organism molecular science
Research Institution	Rikkyo University
Principal Investigator	MAKINO Ryu Rikkyo University, 理学部, 教授 (40101026)
Co-Investigator(Renkei-kenkyūsha)	SHIRO Yoshitugu 独立行政法人理化学研究所, 城生体金属科学研究室, 主任研究員 (70183051) PAKU Sanyou 横浜市立大学, 国際総合科学研究科, 准教授 (20291932)
Project Period (FY)	2007 – 2009
Keywords	活性発現の分子機構
Research Abstract	We have revealed that there were two kinds of nucleotide binding sites, a catalytic and a pseudo-nucleotide sites in soluble guanylate cyclase. When carbon monoxide combined to the enzymic heme, the binding of YC-1 to the pseudo-nucleotide binding site increased the affinity of a nucleotide for the pseudo nucleotide binding site, through interaction between two binding sites. Furthermore, we have first confirmed the formation of the oxygenated form of the enzyme, which was stable under frozen conditions. The formation of the oxygenated form was noted to be regulated by YC-1 binding, and also was suggested to be governed by the deformation of the heme iron from the heme plane, based on the EXAFS analyses.

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