Salicylhydroxamic acid enhances the NADH-oxidase activity of peroxidase in pea mitochondrial and chloroplast suspensions

Salicylhydroxamic acid (SHAM), an alternative oxidase inhibitor of plant mitochondria, enhances the NADH-oxidase activity in mitochondrial and chloroplast suspensions obtained from pea roots or leaves, respectively. This reaction is inhibited by the washing of mitochondria or chloroplasts and is obs...

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Veröffentlicht in:Moscow University biological sciences bulletin 2016, Vol.71 (1), p.19-23
Hauptverfasser: Samuilov, V. D, D. B. Kiselevsky
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description Salicylhydroxamic acid (SHAM), an alternative oxidase inhibitor of plant mitochondria, enhances the NADH-oxidase activity in mitochondrial and chloroplast suspensions obtained from pea roots or leaves, respectively. This reaction is inhibited by the washing of mitochondria or chloroplasts and is observed in supernatants after the removal of the organelles by centrifugation. The reaction is sensitive to CN– and to antioxidant propyl gallate. The NADH oxidation is also enhanced by 2,4-dichlorophenol or phenol, but not salicylic acid. The acceleration of NADH oxidation by phenolic compounds is observed with presence of commercial horseradish peroxidase and is connected with the involvement of these compounds in NADH-dependent peroxidase reaction. SHAM and 2,4-dichlorophenol significantly enhance the destruction of nuclei in guard cells of pea leaf epidermis caused by the generation of reactive oxygen species during the oxidation of exogenous NADH by apoplastic peroxidase.
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identifier ISSN: 0096-3925
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language eng
recordid cdi_crossref_primary_10_3103_S0096392516010089
source SpringerNature Journals
subjects 2,4-dichlorophenol
antioxidants
Biochemistry
Biomedical and Life Sciences
Cell Biology
centrifugation
chloroplasts
guard cells
leaves
Life Sciences
mitochondria
NAD (coenzyme)
oxidation
peas
peroxidase
phenol
Pisum sativum
Plant Sciences
propyl gallate
reactive oxygen species
roots
salicylic acid
washing
Zoology
title Salicylhydroxamic acid enhances the NADH-oxidase activity of peroxidase in pea mitochondrial and chloroplast suspensions
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