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Identification of a novel Arabidopsis thaliana nitric oxide‐binding molecule with guanylate cyclase activity in vitro
Author(s) -
Mulaudzi Takalani,
Ludidi Ndiko,
Ruzvidzo Oziniel,
Morse Monique,
Hendricks Nicolette,
Iwuoha Emmanuel,
Gehring Chris
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.07.023
Subject(s) - cyclic guanosine monophosphate , guanosine , gucy1a3 , gucy1b3 , guanosine monophosphate , biochemistry , chemistry , nitric oxide , heme , gtp' , guanosine triphosphate , arabidopsis , arabidopsis thaliana , enzyme , in vitro , guanylate cyclase 2c , cyclase , nucleotide , gene , organic chemistry , mutant
While there is evidence of nitric oxide (NO)‐dependent signalling via the second messenger cyclic guanosine 3′,5′‐monophosphate (cGMP) in plants, guanylate cyclases (GCs), enzymes that catalyse the formation of cGMP from guanosine 5′‐triphosphate (GTP) have until recently remained elusive and none of the candidates identified to‐date are NO‐dependent. Using both a GC and heme‐binding domain specific (H‐NOX) search motif, we have identified an Arabidopsis flavin monooxygenase (At1g62580) and shown electrochemically that it binds NO, has a higher affinity for NO than for O 2 and that this molecule can generate cGMP from GTP in vitro in an NO‐dependent manner.