The roles of cysteines in the heme domain of human soluble guanylate cyclase

• Published in: Chinese chemical letters Vol. 23; no. 8; pp. 973 - 976
• Main Authors: Zhong, Fang Fang, Liu, Xiao Xiao, Pan, Jie, Huang, Zhong Xian, Tan, Xiang Shi
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.08.2012; Department of Chemistry,Fudan University,Shanghai 200433,China%Department of Chemistry,Fudan University,Shanghai 200433,China; Institutes of Biomedical Sciences,Fudan University,Shanghai 200433,China
• Subjects: Cysteine; Dimerization; Heme domain; Human soluble guanylate cyclase; sGC; 二聚化; 凝胶过滤; 半胱氨酸; 可溶性鸟苷酸环化酶; 定向突变; 生物活性; 素域; 血红素; Cysteine; Dimerization; Human soluble guanylate cyclase; sGC; Heme domain
• ISSN: 1001-8417; 1878-5964
• DOI: 10.1016/j.cclet.2012.06.005

Soluble guanylate cyclase（sGC） is a critical heme-containing enzyme involved in NO signaling.The dimerization of sGC subunits is necessary for its bioactivity and its mechanism is a striking and an indistinct issue.The roles of heme domain cysteines of the sGC on the dimerization and heme binding were investigated herein.The site-directed mutations of three conserved cysteines（C78A,C122A and C174S） were studied systematically and the three mutants were characterized by gel filtration analysis,UV-vis spectroscopy and heme transfer examination.Cys78 was involved in heme binding but not referred to the dimerization,while Cys174 was demonstrated to be involved in the homodimerization.These results provide new insights into the cysteine-related dimerization regulation of sGC.