4.7 Article

Species-specific enzymatic tolerance of sulfide toxicity in plant roots

Journal

PLANT PHYSIOLOGY AND BIOCHEMISTRY
Volume 88, Issue -, Pages 36-41

Publisher

ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.plaphy.2015.01.007

Keywords

Alcohol dehydrogenase; Cytochrome c oxidase; Estuarine plants; Flooding-sensitive plants; Flooding-tolerant plants; Respiration Sulfide

Categories

Funding

  1. Kansas Academy of Science Student Research Grant
  2. National Center for Research Resources [P20RR016475]
  3. National Institute of General Medical Sciences from the National Institutes of Health [P20GM103418]

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Toxic effects of sulfide come from a poisoning of a number of enzymes, especially cytochrome c oxidase, which catalyzes the terminal step in mitochondrial aerobic respiration. Despite this, some estuarine plants live in sulfide-rich sediments. We hypothesized estuarine and flooding-tolerant species might be more tolerant of sulfide compared to upland species, and this was tested by measures of root cytochrome c oxidase and alcohol dehydrogenase activities in extracts exposed to sulfide. Enzyme activities were measured in 0, 5, 10, 15, and 20 mu M sodium sulfide, and compared among 17 species of plants. Activities of alcohol dehydrogenase and cytochrome c oxidase were both reduced by increasing sulfide concentration, but cytochrome c oxidase was more sensitive to sulfide compared to alcohol dehydrogenase. Activities of cytochrome c oxidase were reduced to near zero at 5-10 mu M sulfide whereas alcohol dehydrogenase activities were only reduced by about 50% at 10 mu M sulfide. All species were sensitive to increasing sulfide, but to different degrees. Cytochrome c oxidase in flooding-sensitive species was decreased to near zero activity at 5 mu M sulfide, whereas activities in some flooding-tolerant species were still detectable until 15 mu M sulfide. Cytochrome c oxidase activities in some estuarine species were low even in the absence of sulfide, perhaps an adaptation to avoid sulfide vulnerability in their native, sulfide-rich habitat. This illustrates the potent metabolic effects of sulfide, and this is the first demonstration of varying sensitivities of cytochrome c oxidase to sulfide across organisms, making these data of novel importance. (C) 2015 Elsevier Masson SAS. All rights reserved.

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