http://purl.uniprot.org/citations/16331987 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16331987 | http://www.w3.org/2000/01/rdf-schema#comment | "Soluble guanylate cyclase (sGC) is a heterodimeric, nitric oxide (NO)-sensing hemoprotein composed of two subunits, alpha1 and beta1. NO binds to the heme cofactor in the beta1 subunit, forming a five-coordinate NO complex that activates the enzyme several hundred-fold. In this paper, the heme domain has been localized to the N-terminal 194 residues of the beta1 subunit. This fragment represents the smallest construct of the beta1 subunit that retains the ligand-binding characteristics of the native enzyme, namely, tight affinity for NO and no observable binding of O(2). A functional heme domain from the rat beta2 subunit has been localized to the first 217 amino acids beta2(1-217). These proteins are approximately 40% identical to the rat beta1 heme domain and form five-coordinate, low-spin NO complexes and six-coordinate, low-spin CO complexes. Similar to sGC, these constructs have a weak Fe-His stretch [208 and 207 cm(-)(1) for beta1(1-194) and beta2(1-217), respectively]. beta2(1-217) forms a CO complex that is very similar to sGC and has a high nu(CO) stretching frequency at 1994 cm(-)(1). The autoxidation rate of beta1(1-194) was 0.073/min, while the beta2(1-217) was substantially more stable in the ferrous form with an autoxidation rate of 0.003/min at 37 degrees C. This paper has identified and characterized the minimum functional ligand-binding heme domain derived from sGC, providing key details toward a comprehensive characterization."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi051601b"xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/author | "Pan D."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/author | "Marletta M.A."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/author | "Davis J.H."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/author | "Behrends S."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/author | "Karow D.S."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/author | "Mathies R.A."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/pages | "16266-16274"xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/title | "Characterization of functional heme domains from soluble guanylate cyclase."xsd:string |
http://purl.uniprot.org/citations/16331987 | http://purl.uniprot.org/core/volume | "44"xsd:string |
http://purl.uniprot.org/citations/16331987 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16331987 |
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