The role of coenzymes in dehydrogenase systems

Dixon, Malcolm; Zerfas, L. G.

doi:10.1042/bj0340371

Cited by 27 publications

(5 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The total 02 outputs were close to theory in all cases (Table 5) It is well known that quinones formed by the action of polyphenol oxidase can bring about secondary oxidations, e.g. coenzyme I (Dixon & Zerfas, 1940), coenzyme II (Kubowitz, 1937), ascorbic acid (Robinson & Nelson, 1944), aminoacids (Happold & Raper, 1925;James, Roberts, Beevers & De Kock, 1948). Evidence has been presented that tyrosinase may act as a terminal oxidase in plant respiration, the quinone acting as a hydrogen acceptor (e.g.…”

Section: Experimental and Resultsmentioning

confidence: 86%

The oxidation of manganese by peroxidase systems

Kenten

Mann

1950

Biochemical Journal

View full text Add to dashboard Cite

Section: Experimental and Resultsmentioning

confidence: 86%

The oxidation of manganese by peroxidase systems

Kenten

Mann

1950

Biochemical Journal

View full text Add to dashboard Cite

“…Boswell &;Whiting, 1938;Baker & Nelson, 1943). Since quinones oxidize coenzyme I (Dixon & Zerfas, 1940) and coenzyme II (Kubowitz, 1937), tyrosinase could thus act as a link between oxygen and dehydrogenases requiring these coenzymes. In a similar manner peroxidase could link enzymes producing hydrogen peroxide to such dehydrogenase systems.…”

Section: Discussionmentioning

confidence: 99%

The action of peroxidase systems on ferrocyanide, molybdate, tungstate and vanadate

Kenten

Mann

1951

Biochemical Journal

View full text Add to dashboard Cite

Kenten & Mann (1950) showed that plant peroxidase preparations in the presence of certain phenolic substrates catalyse the oxidation of Mn++ by hydrogen peroxide. Evidence was obtained that the Mn++ reduces an intermediate oxidation product of the phenolic substrate and thereby is itself oxidized. The oxidizing capabilities of the system peroxidase + phenolic substrate + hydrogen peroxide towards inorganic compounds have now been further investigated. It is shown that the system oxidizes ferrocyanide, and evidence suggesting the oxidation of molybdate, tungstate and vanadate is reported. MATERIALS AND METHODS Peroxida8e preparation8 were obtained from horseradish by the method of Keilin & Mann (1937). The 'Purpurogallinzahl' (P.Z.) of these preparations was determined by the method of Keilin & Mann (1937). Hydroge.n peroxide. In the experiments with molybdate, tungstate and vanadate, approximately 0-05M-H,0, was used, and for the manometric experiments with ferrocyanide approximately 0-025M-H202 in 0-0105m-NaHCO.,. Fresh solutions were prepared for each experiment. The 0-025M-HSOS in NaHCO, was estimated by KMnO, titration and the 0-05m-H202 manometrically with MnO2 in acid solution (Kenten & Mann, 1950). Ammonium permolybdate was prepared by treatment of 100 vol. H202 with molybdate according to the method of

show abstract

“…69 Th ey speak of ' the extremes of economic inequality that have become commonplace in liberal democracies throughout the world[,] poverty … on the rise in the developed world [, and] the stagnation of wages and economic insecurity ' . 70 Th ey bring this description to life through intuitive reasoning about what it means ' [w]hen individuals who are born poor cannot become rich, and vice versa ' . 71 In Dixon and Suk ' s estimation, that status quo 72 Ibid.…”

Section: Modern-day Backslidingmentioning

confidence: 99%

The Abolition of Class Government

Kuhner

2020

SSRN Journal

View full text Add to dashboard Cite

The role of coenzymes in dehydrogenase systems

Cited by 27 publications

References 11 publications

The oxidation of manganese by peroxidase systems

The oxidation of manganese by peroxidase systems

The action of peroxidase systems on ferrocyanide, molybdate, tungstate and vanadate

The Abolition of Class Government

Contact Info

Product

Resources

About