Publication | Open Access
Identification of a novel <i>Arabidopsis thaliana</i> nitric oxide-binding molecule with guanylate cyclase activity <i>in vitro</i>
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Citations
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References
2011
Year
Plant Molecular BiologyGuanylate Cyclase ActivityBiosynthesisArabidopsis Flavin MonooxygenaseEngineeringBiochemistryReactive Nitrogen SpecieNitric OxideNatural SciencesNitrosative StressMolecular BiologyPlant BiochemistryRedox BiologySearch MotifPlant PhysiologyPlant Hormone
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.
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