rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5
|
pubmed:dateCreated |
1998-8-25
|
pubmed:abstractText |
Nitric oxide (.NO) is used in biology as both an intercellular signaling agent and a cytotoxic agent. In signaling, submicromolar quantities of .NO stimulate the soluble isoform of guanylate cyclase (sGC) in the receptor cell. .NO increases the Vmax of this heterodimeric hemoprotein up to 400-fold by interacting with the heme moiety of sGC to form a 5-coordinate complex. Carbon monoxide (CO) binds to the heme to form a 6-coordinate complex, but only activates the enzyme 5-fold, YC-1 is a recently discovered compound that relaxes vascular smooth muscle by stimulating sGC.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
1074-5521
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
5
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
255-61
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
|
pubmed:year |
1998
|
pubmed:articleTitle |
Synergistic activation of soluble guanylate cyclase by YC-1 and carbon monoxide: implications for the role of cleavage of the iron-histidine bond during activation by nitric oxide.
|
pubmed:affiliation |
Department of Biological Chemistry, School of Medicine, University of Michigan, Ann Arbor 48109-1065, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|