Studies on the Effect of Temperature on the Catalase Reaction

Morgulis, Sergius; Beber, Meyer; Rabkin, I.

doi:10.1016/s0021-9258(18)84619-1

Cited by 10 publications

(2 citation statements)

References 4 publications

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“…The relation between temperature and protein structure has been under investigation using different protein [1] and short peptide [2] models, since early reports of the loss in catalytic activity of isolated proteins at high temperatures [3]. Proteins exist in equilibrium between folded and unfolded states [4], and in most proteins, the relative fractions of their folded states predominate at functional temperatures, while the unfolded state fractions increase with temperature and predominate at high temperatures.…”

Section: Figmentioning

confidence: 99%

α‐Helices propagating from stable nucleators exhibit unconventional thermal folding

2021

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Although the effect of thermal perturbations on protein structure has long been modeled in helical peptides, several details, such as the relation between the thermal stabilities of the propagating and nucleating segments of helices, remain elusive. We had earlier reported on the helix‐nucleating propensities of covalent H‐bond surrogate‐constrained α‐turns. Here, we analyze the thermal stabilities of helices that propagate along peptides appended to these α‐helix nucleators using their NMR and far‐UV CD spectra. Unconventional thermal folding of these helix models reveals that the helical fold in propagating backbones resists thermal perturbations as long as their nucleating template is intact. The threshold temperature of such resistance is also influenced by the extent of similarity between the natures of helical folds in the nucleating and propagating segments. Correlations between helicities and rigidities of helix‐nucleating and helix‐propagating segments reveal subtle interdependence, which explains cooperativity and residual helix formation during protein folding.

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Section: Figmentioning

confidence: 99%

α‐Helices propagating from stable nucleators exhibit unconventional thermal folding

2021

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“…Temperatures above 20°C is responsible for the spontaneous inactivation of the enzyme by heat leading to diminished catalase activity 31 . Rady et al, 33 reported that Synechocystis PCC 6803 strain acclimated at different growth temperature exhibited significantly increased catalase activity at 20°C and decreased significantly when growth temperature was increased to 43°C.…”

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Effects of Various Physico-chemical Parameters on Growth, Morphology and Physiology of a Thermophilic Cyanobacterium Fischerella thermalis (Schwabe) Gomont

Roy,

Bhattacharya,

Ray

2016

J. Adv. Mircobiol.

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The growth as well as morphological and physiological features of thermophilic cyanobacteria vary greatly depending upon the physico-chemical factors prevailing in the water of hot springs. Effects of some physico-chemical parameters of water like-temperature, pH, nitrate and phosphate contents were observed on a thermophilic cyanobacterium Fischerella thermalis isolated from a hot water spring located at Panifala, Burdwan, West Bengal. Catalase activity under varying temperatures and light intensities was also studied in in vitro condition. Filaments incubated at 45 o -55 o C temperature, acidic (5.0-7.0) and highly alkaline (10.0) pH, high concentration (1.0-2.0 g/L) of NaNO 3 and low (0-0.02 g/L) as well as high concentration (0.1 g/L) of K 2 HPO 4 showed various morphological abnormalities like shrinkage of cells, degradation of cellular contents, twisted and broken trichomes, discolouration of filaments, empty filaments. Such variations in physical and chemical factors also resulted in variations in protein, carbohydrate, chlorphyll-a and carotenoid contents. Heterocyst frequency and branching frequency was highest at 37 o C temperature, 8.0-9.0 pH and 0.06 g/L of K 2 HPO 4 concentration. At increasingly high concentration of NaNO 3 branching frequency increased but heterocyst frequency decreased. 37 o C temperature, pH 8.0, 1.0 g/L NaNO 3 and 0.06 g/L of K 2 HPO 4 concentration were found to be ideal for growth in in vitro condition. High light intensity (75 photons m -2 s -1 ) and low temperature (25 o C) were observed to be responsible for increased catalase activity. This investigation will help to optimize the culture medium for in vitro production of biologically significant organisms like filamentous thermophilic cyanobacteria and throw light on experimental taxonomy.

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Die Katalasen

Euler¹,

Zeile²

1934

Die Katalasen Und Die Enzyme Der Oxydation Und Reduktion

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Studies on the Effect of Temperature on the Catalase Reaction

Cited by 10 publications

References 4 publications

α‐Helices propagating from stable nucleators exhibit unconventional thermal folding

α‐Helices propagating from stable nucleators exhibit unconventional thermal folding

Effects of Various Physico-chemical Parameters on Growth, Morphology and Physiology of a Thermophilic Cyanobacterium Fischerella thermalis (Schwabe) Gomont

Die Katalasen

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