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    Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro

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    Type
    Article
    Authors
    Mulaudzi, Takalani
    Ludidi, Ndiko N.
    Ruzvidzo, Oziniel
    Morse, Monique V.
    Hendricks, Nicolette R.
    Iwuoha, Emmanuel Iheanyichukwu
    Gehring, Christoph A cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Molecular Signalling Group
    Date
    2011-07-31
    Online Publication Date
    2011-07-31
    Print Publication Date
    2011-09-02
    Permanent link to this record
    http://hdl.handle.net/10754/561865
    
    Metadata
    Show full item record
    Abstract
    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.
    Citation
    Mulaudzi, T., Ludidi, N., Ruzvidzo, O., Morse, M., Hendricks, N., Iwuoha, E., & Gehring, C. (2011). Identification of a novel Arabidopsis thaliana nitric oxide-binding molecule with guanylate cyclase activity in vitro. FEBS Letters, 585(17), 2693–2697. doi:10.1016/j.febslet.2011.07.023
    Sponsors
    This work was supported by the South African National Research Foundation.
    Publisher
    Wiley
    Journal
    FEBS Letters
    DOI
    10.1016/j.febslet.2011.07.023
    PubMed ID
    21820435
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.febslet.2011.07.023
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program

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