期刊
FEBS LETTERS
卷 585, 期 17, 页码 2693-2697出版社
WILEY
DOI: 10.1016/j.febslet.2011.07.023
关键词
Affinity; Cyclic voltammetry; Guanylate cyclase; H-NOX domain; Nitric oxide; Oxygen; Square wave voltammetry; Arabidopsis thaliana
资金
- South African National Research Foundation
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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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