Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Electron spin resonance study of the role of NO. catalase in the activation of guanylate cyclase by NaN/sub 3/ and NH/sub 2/OH

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:5308355

The role of NO.catalase in the activation of partially purified soluble guanylate cyclase of rat liver by NaN/sub 3/ and NH/sub 2/OH was examined by electron spin resonance (ESR) spectroscopy. The stimulation of partially purified guanylate cyclase by NO.catalase was similar to that obtained with NO.hemeoglobin and with NO.cytochrome P-420. By contrast, these same enzyme preparations did not respond to NO or catalase alone. Addition of hematin or hemoglobin plus a reducing agent to purified guanylate cyclase restored enzyme responsiveness to NO and N-methyl-N'-nitro-N-nitro-soguanidine (MNNG), but not to NaN/sub 3/ or NH/sub 2/OH. Formation of the NO.catalase complex was evident by ESR spectroscopy in test solutions containing NaN/sub 3/ or NH/sub 2/OH, catalase, and a glucose-glucose oxidase, H/sub 2/O/sub 2/-generating system. These results provide evidence for catalase-dependent NO generation from NaN/sub 3/ and NH/sub 2/OH under conditions leading to guanylate cyclase activation. Preformed NO.hemoglobin or NO.cytochrome P-420 also activated heme-deficient partially purified guanylate cyclase. In the absence of the NO ligand, both hemoglobin and catalase suppress the stimulatory effects of the corresponding NO.heme proteins on guanylate cyclase. However, hemoglobin is approximately 2000 times more effective as an inhibitor of NO.hemoglobin stimulation of guanylate cyclase than is catalase as an inhibitor of NO.catalase action.The results imply that guanylate cyclase responses to activators that can form NO are determined by both the stimulatory activity of the endogenous heme acceptors of NO and the relative inhibitory effects of the unliganded heme proteins present. (DS)

Research Organization:
Univ. of Pittsburgh, PA
OSTI ID:
5308355
Journal Information:
J. Biol. Chem.; (United States), Journal Name: J. Biol. Chem.; (United States) Vol. 254:17; ISSN JBCHA
Country of Publication:
United States
Language:
English