The promoter region of the Zinnia elegans basic peroxidase isoenzyme gene contains cis-elements responsive to nitric oxide and hydrogen peroxide

Planta ◽  
2012 ◽  
Vol 236 (2) ◽  
pp. 327-342 ◽  
Author(s):  
Laura V. Gómez-Ros ◽  
Carlos Gabaldón ◽  
María José López Núñez-Flores ◽  
Jorge Gutiérrez ◽  
Joaquín Herrero ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Peroxide ◽  
Promoter Region ◽  
Zinnia Elegans ◽  
Cis Elements ◽  
Peroxidase Isoenzyme

Effects of Exogenous Abscisic Acid,Nitric Oxide and Hydrogen Peroxide on Stomatal Movement in Petals and Leaves ofZephyranthes candida

2013 ◽  
Vol 31 (3) ◽  
pp. 278
Author(s):  
Wen-Qi XIE ◽  
Jin-Ping ZHANG ◽  
Jian-Yi TAN ◽  
Xiao-Li XUAN ◽  
Yong-Fei WANG ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Peroxide ◽  
Abscisic Acid ◽  
Stomatal Movement

scholarly journals Hydrogen peroxide and nitric oxide as signalling molecules in plants

2002 ◽  
Vol 53 (372) ◽  
pp. 1237-1247 ◽  
Author(s):  
Steven J. Neill ◽  
Radhika Desikan ◽  
Andrew Clarke ◽  
Roger D. Hurst ◽  
John T. Hancock
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Peroxide ◽  
Signalling Molecules

scholarly journals Cloning, Expression, and Purification of a Nitric Oxide Synthase-Like Protein fromBacillus cereus

2010 ◽  
Vol 2010 ◽  
pp. 1-4 ◽  
Author(s):  
Heather J. Montgomery ◽  
Andrea L. Dupont ◽  
Hilary E. Leivo ◽  
J. Guy Guillemette
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Peroxide ◽  
Nitric Oxide Synthase ◽  
Expression And Purification ◽  
Spectral Shifts ◽  
Reconstituted System ◽  
Low Levels ◽  
And Function ◽  
Oxide Synthase ◽  
Reductase Domain

The nitric oxide synthase-like protein fromBacillus cereus(bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer. The recombinant protein showed similar spectral shifts to the mammalian NOS proteins and could bind the substrates L-arginine andNG-hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation ofNG-hydroxy-L-arginine and L-arginine by bcNOS, while a reconstituted system with the rat neuronal NOS reductase domain showed no activity. The recombinant bcNOS protein adds to the complement of bacterial NOS-like proteins that are used for the investigation of the mechanism and function of NO in microorganisms.

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