Properties of azide-catalase

Keilin, D.; Hartree, E. F.

doi:10.1042/bj0390148

Cited by 99 publications

(48 citation statements)

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“…Theorell & Ehrenberg (1952b) discussed the nature of the azide reactions, but their suggestions conflicted with the data of Foulkes & Lemberg (1949) and Keilin & Hartree (1954). In particular, although Theorell & Ehrenberg (1952b) claimed that the major product formed during the oxidation of azide is nitrous oxide, the latter groups of workers agree in postulating the production of sufficient quantities of nitric oxide to form the observed ferrous derivative of the enzyme which, according to Keilin & Hartree (1954) oxide-ferrocatalase, catalase * Fe2+NO. It is therefore not clear which is the main reaction, or what side reactions may occur.…”

Section: +02+1h20 (Lb)mentioning

confidence: 74%

“…(1) was recognized. Subsequently it wa-s discovered that the reaction with azide involves a peroxidatic attack of compound I on azide (Chance, 1947) giving rise to a multiplicity of oxidation products including nitrous oxide and nitrogen (Theorell & Ehrenberg, 1952b) together with small amounts of nitric oxide (Keilin & Hartree, 1954). Theorell & Ehrenberg (1952b) discussed the nature of the azide reactions, but their suggestions conflicted with the data of Foulkes & Lemberg (1949) and Keilin & Hartree (1954).…”

Section: +02+1h20 (Lb)mentioning

confidence: 98%

“…Subsequently it wa-s discovered that the reaction with azide involves a peroxidatic attack of compound I on azide (Chance, 1947) giving rise to a multiplicity of oxidation products including nitrous oxide and nitrogen (Theorell & Ehrenberg, 1952b) together with small amounts of nitric oxide (Keilin & Hartree, 1954). Theorell & Ehrenberg (1952b) discussed the nature of the azide reactions, but their suggestions conflicted with the data of Foulkes & Lemberg (1949) and Keilin & Hartree (1954). In particular, although Theorell & Ehrenberg (1952b) claimed that the major product formed during the oxidation of azide is nitrous oxide, the latter groups of workers agree in postulating the production of sufficient quantities of nitric oxide to form the observed ferrous derivative of the enzyme which, according to Keilin & Hartree (1954) oxide-ferrocatalase, catalase * Fe2+NO.…”

Section: +02+1h20 (Lb)mentioning

confidence: 99%

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The reactions of azide with catalase and their significance

Nicholls¹

1964

Biochemical Journal

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Section: +02+1h20 (Lb)mentioning

confidence: 74%

Section: +02+1h20 (Lb)mentioning

confidence: 98%

Section: +02+1h20 (Lb)mentioning

confidence: 99%

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The reactions of azide with catalase and their significance

Nicholls¹

1964

Biochemical Journal

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“…This can be calculated from the Kat.-f. values of the pure enzyme (95,000) and the lyzed bacteria (800-1800 in different batches), giving a catalase content for this organism of 1-2 % of its dry weight. This is about ten times the catalase content of human red blood corpuscles (Herbert & Pinsent, 1948 Keilin & Hartree (1936, 1945b suggests, catalase has other functions besides the simple decomposition of hydrogen peroxide. SUMMARY 1.…”

Section: Discussionmentioning

confidence: 99%

“…Once the molecular weight and Kat.-f. of the pure enzyme are known, it is possible to calculate the 'Turnover Number', defined by Warburg & Christian (1933) Coupled oxidation of alcohoil Keilin & Hartree (1936, 1945b have shown that if catalase and ethanol are added to any enzyme system which produces hydrogen peroxide, the latter is used by the catalase to bring about a 'coupled oxidation' of the ethanol to acetaldehyde. In other words, under these special conditions (continuous slow supply of hydrogen peroxide at a very low concentration), the catalase acts as a peroxidase.…”

Section: Methodsmentioning

confidence: 99%

Crystalline Bacterial Catalase

Herbert

Pinsent

1947

Nature

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spectroscope the narrow width of the absorption band in the red led to an overestimate of its intensity. Others have also been misled by the narrowness of the first absorption band; thus Grinstein, Schwartz & Watson (1945) describe the relative intensities of the absorption bands of coproporphyrin I as IV, III, I and II in decreasing order.The eluate containing the second porphyrin zone was evaporated to dryness, and after recrystallization from chloroform and methanol gave 7-1 mg. of the typical hairlike crystals of uroporphyrin I octamethyl ester (m.p. 288°). In chloroform, this ester showed absorption bands at 625-7, 576-7, 536-5 and 503-6 mi., intensity IV>III>II>I (Hartridge reversion spectroscope). The third porphyrin zone has not yet been identified. DISCUSSIONThe isolation of coproporphyrin III ester in relatively enormous quantities in the large-scale production of purified diphtheria toxoid provides an abundant and hitherto unexplored source of coproporphyrin III, which wiU be of the greatest value in the investigation of the metabolic relationships of this material in the intact animal. The production of small quantities of uroporphyrin I provides yet another example of the so-called dualism of the porphyrins, attention to which was first drawn by Fischer (1937). In the light of present knowledge it is not possible to speculate on the significance of this dualism to the economy of the organism. The implications suggested by Pappenheimer (1947) regarding the relationship of the production of porphyrin to toxin formation will be the subject of a separate paper to be published elsewhere. SUMMARYCoproporphyrin III tetramethyl ester in large yield and uroporphyrin I octamethyl ester in very small yield have been prepared from toxic culture filtrates of Corynebacterium diphtheriae.

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End Group Analysis of Polysaccharides

Montgomery

Smith

1956

Methods of Biochemical Analysis

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Properties of azide-catalase

Cited by 99 publications

References 12 publications

The reactions of azide with catalase and their significance

The reactions of azide with catalase and their significance

Crystalline Bacterial Catalase

End Group Analysis of Polysaccharides

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