TY - JOUR
T1 - Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro
AU - Mulaudzi, Takalani
AU - Ludidi, Ndiko N.
AU - Ruzvidzo, Oziniel
AU - Morse, Monique V.
AU - Hendricks, Nicolette R.
AU - Iwuoha, Emmanuel Iheanyichukwu
AU - Gehring, Christoph A
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: This work was supported by the South African National Research Foundation.
PY - 2011/7/31
Y1 - 2011/7/31
N2 - 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. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
AB - 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. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
UR - http://hdl.handle.net/10754/561865
UR - http://doi.wiley.com/10.1016/j.febslet.2011.07.023
UR - http://www.scopus.com/inward/record.url?scp=81155151023&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2011.07.023
DO - 10.1016/j.febslet.2011.07.023
M3 - Article
C2 - 21820435
SN - 0014-5793
VL - 585
SP - 2693
EP - 2697
JO - FEBS Letters
JF - FEBS Letters
IS - 17
ER -