Photoinactivation of catalase in vitro and in leaves

Feierabend, J.; Engel, Stanislav

doi:10.1016/0003-9861(86)90365-6

Cited by 137 publications

(83 citation statements)

References 28 publications

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“…When potential repair of catalase degradation through new synthesis was blocked by the application of the protein synthesis inhibitor CHI, photoinactivation became apparent, particularly in A. halimus leaves. Relative to results obtained for several non-desert plants in the presence of translation inhibitors (Feierabend & Engel 1986), the rate of catalase photoinactivation was low, both in R. raetam and A. halimus, suggesting that it was efficiently avoided in vivo. However, when the light exposure was performed at high temperature a considerably larger decline of the catalase activity than in the presence of CHI was induced in A. halimus, but not in R. raetam.…”

Section: Discussioncontrasting

confidence: 81%

“…Because in cell-free extracts of the two plants catalase activity was in vitro similarly susceptible to photoinactivation (Fig. 2), as catalases from other sources (Björn 1969;Cheng, Kellogg & Packer 1981;Feierabend & Engel 1986), these desert plants must be endowed with specific mechanisms of adaptation, in order to avoid or prevent apparent losses of catalase activity under natural conditions. Attempts were made to elucidate mechanisms that contribute to the extraordinary in vivo stability of catalase in the two desert species.…”

Section: Discussionmentioning

confidence: 99%

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Light stress effects and antioxidative protection in two desert plants

1997

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1. The enzyme catalase was investigated as a sensitive marker of light stress in Retama raetam stems and Atriplex halimus leaves. While the activity of catalase was readily photoinactivated in vitro when crude extracts from these tissues were exposed to a photon flux of 500μmolm–2s–1 photosynthetic active radiation (PAR), no apparent losses of the extractable catalase activities were observed when tissues were harvested from desert plants at noon when light levels were as high as 2200μmolm–2s–1 PAR. 2. When stems of R. raetam or leaves of A. halimus were exposed to natural daylight of 1000μmolm–2s–1 PAR in the presence of cycloheximide (CHI), in order to prevent the new synthesis of catalase, or at a temperature of 42–44°C, only minor losses of catalase activity occurred in stems of R. raetam, but a marked apparent photoinactivation of catalase was observed in leaves of A. halimus. 3. Similarly, stronger declines of the ratio Fv/Fm, indicating more severe photoinhibition of photosystem II (PSII), were observed in A. halimus, compared with R. raetam. 4. For R. raetam, activities of some antioxidative enzymes and the carotenoid contents were higher in plants growing in the desert than in plants collected from non‐desert locations. 5. During the daily increase of light and temperature the antioxidants ascorbate and glutathione became more oxidized and violaxanthin was converted to zeaxanthin in R. raetam stems, while these antioxidants became more reduced and zeaxanthin was not notably accumulated in A. halimus leaves. 6. The results suggest that the desert plants R. raetam and A. halimus apply different strategies of protection against light‐stress damage. In the stems of R. raetam antioxidative protection appears to play the major role, while A. halimus appears to avoid light damage in the field by the mutual shading of leaves and reflection of light at the leaf surface.

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Section: Discussioncontrasting

confidence: 81%

Section: Discussionmentioning

confidence: 99%

Light stress effects and antioxidative protection in two desert plants

1997

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“…Lead decreased the activity of CAT in the shoot only in the Raphanus sativus at lower Pb concentrations. However, with increasing Pb level, reduction in CAT activity was observed, which has been attributed to the activation of the enzyme protein (Feieraband and Engel, 1986) and the decrease in enzyme synthesis (Mittler, 2002). The decrease in CAT activity could indicate its inactivation by accumulation of H 2 O 2 induced by lead in Cassia angustifolia (Qureshi et al, 2007).…”

Section: Pb Effects On Antioxidant Enzymementioning

confidence: 99%

Oxidative Stress Induction by Lead in Leaves of Radish (Raphanus sativus) Seedlings

et al. 2011

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Oxidative stress was induced by lead acetate (Pb) in Raphanus sativus seedlings grown in a hydroponic system using sand as substrate. Thirty day old acclimated seeds were treated for 7 days with five Pb levels (0 as control, 100, 200, 500 and 1000 mg l -1 ). Parameters such as growth, oxidative damage markers (lipid peroxidation, protein oxidation and hydrogen peroxide contents) and enzymatic activities of catalase (CAT) and peroxidase (POD) were investigated. Lead concentration in plant tissues increased with increasing of Pb levels. Shoot fresh weight, chlorophyll and carotenoid concentration were significantly decreased at 100 mg l -1 Pb. Lipid peroxidation, protein oxidation and H 2 O 2 levels were increased at 500 and 1000 mg l -1 Pb compared to control treatment, in shoots. Peroxidase activity showed a straight correlation with H 2 O 2 concentration, whereas CAT activity decreased only in shoots. These changes in enzymatic and non-enzymatic antioxidants showed that the Pb exposition had a significant disturbance on Raphanus sativus plantlets and affect the biochemical and physiological processes.

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“…developed a multiplicity of antioxidative mechanisms (3,27), some components are obviously not fully protected from photodamage. Thus, the enzyme catalase is light sensitive in vitro and suffers from photoinactivation with subsequent degradation in intact leaves as well (7,12,31). To maintain a constant catalase level in light, its loss has to be continuously compensated for by an adequate concomitant resynthesis of the enzyme (12).…”

mentioning

confidence: 99%

“…To maintain a constant catalase level in light, its loss has to be continuously compensated for by an adequate concomitant resynthesis of the enzyme (12). When, however, light degradation exceeds the capacity for repair (25) or when resynthesis is impaired by inhibitors (7) or by stress conditions such as low temperature (31), an apparent loss of catalase is observed. The velocity of loss depends on light intensity.…”

mentioning

confidence: 99%

Photoinactivation of Catalase Occurs under Both High- and Low-Temperature Stress Conditions and Accompanies Photoinhibition of Photosystem II

Feierabend¹,

Schaan²,

Hertwig³

1992

Plant Physiol.

179

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Severe photoinactivation of catalase (EC 1.11.1.6) and a decline of variable fluorescence (FJ), indicating photoinhibition of photosynthesis, were observed as rapid and specific symptoms in leaves exposed to a high heat-shock temperature of 40°C as well as in leaves exposed to low chilling temperatures in white light of only moderately high photosynthetic photon flux density of 520 ME m-2 s-'. Other parameters, such as peroxidase (EC 1.11.1.7), glycolate oxidase (EC 1.1.3.1), glutathione reductase (EC 1.6.4.2), or the chlorophyll content, were hardly affected under these conditions. At a compatible temperature of 22°C, the applied light intensity did not induce severe photoinactivations. In darkness, exposures to high or low temperatures did not affect catalase levels. Also, decline of F, in light was not related to temperature sensitivity in darkness. The effective low-temperature ranges inducing photoinactivation of catalase differed significantly for chilling-tolerant and chilling-sensitive plants. In leaves of rye (Secale cereale L.) and pea (Pisum sativum L.), photoinactivation occurred only below 15°C, whereas inactivation occurred at 15°C in cucumber (Cucumis sativus L.) and maize (Zea mays L.). The behavior of F, was similar, but the difference between chilling-sensitive and chillingtolerant plants was less striking. Whereas the catalase polypeptide, although photoinactivated, was not cleaved at 0 to 4°C, the Dl protein of photosystem 11 was greatly degraded during the lowtemperature treatment of rye leaves in light. Rye leaves did not exhibit symptoms of any major general photodamage, even when they were totally depleted of catalase after photoinactivation at 0 to 4°C, and catalase recovered rapidly at normal temperature. In cucumber leaves, the decline of catalase after exposures to bright light at 0 to 4°C was accompanied by bleaching of chlorophyll, and the recovery observed at 25°C was slow and required several days. Similar to the Dl protein of photosystem 11, catalase differs greatly from other proteins by its inactivation and high turnover in light. Inasmuch as catalase and Di protein levels depend on continuous repair synthesis, preferential and rapid declines are generally to be expected in light whenever translation is suppressed by stress actions, such as heat or chilling, and recovery will reflect the repair capacity of the plants.

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Photoinactivation of catalase in vitro and in leaves

Cited by 137 publications

References 28 publications

Light stress effects and antioxidative protection in two desert plants

Light stress effects and antioxidative protection in two desert plants

Oxidative Stress Induction by Lead in Leaves of Radish (Raphanus sativus) Seedlings

Photoinactivation of Catalase Occurs under Both High- and Low-Temperature Stress Conditions and Accompanies Photoinhibition of Photosystem II

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