Spectrophotometric determination of thiocyanate with rhenium

Neas, Robert E.; Guyon, John C.

doi:10.1021/ac60280a039

Cited by 8 publications

(3 citation statements)

References 17 publications

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“…Thiocyanate determination. The amount of thiocyanate released on cyanide inactivation of known amounts of enzyme was measured by a modification (Cleere & Coughlan, 1974a) of the method of Neas & Guyon (1969) and was used as a measure of the degree of functionality of the enzyme samples employed (see Edmonson et al, 1972).…”

Section: Methodsmentioning

confidence: 99%

Turkey liver xanthine dehydrogenase: properties of the enzyme dependent on the content of functional active sites (Short Communication)

Cleere

O'Regan

Coughlan

1974

Biochemical Journal

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Turkey liver xanthine dehydrogenase containing the full complement of molybdenum, flavin and iron-sulphur prosthetic groups is, as normally isolated, a mixture of functional and non-functional enzyme. The latter apparently lacks the cyanolysable persulphide groups essential to the oxidation of xanthine and to interaction with arsenite. These groups are not required for the oxidation of NADH by Methylene Blue. That KI treatment effects a differential release of flavin from xanthine-prereduced and NADH-prereduced enzyme merely reflects the degree of functionality of the preparations used and may not be taken as evidence for non-equivalence of the flavin chromophores.

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Section: Methodsmentioning

confidence: 99%

Turkey liver xanthine dehydrogenase: properties of the enzyme dependent on the content of functional active sites (Short Communication)

Cleere

O'Regan

Coughlan

1974

Biochemical Journal

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“…Thiocyanate was measured spectrophotometrically as the rhenium complex by a modification of the method of Neas & Guyon (1969). Cyanide-inactivated enzyme (see Fig.…”

Section: Thiocyanate Determinationmentioning

confidence: 99%

“…To this was added 0.025ml of KReO4 (4.0mM), 0.175ml of conc. HCl and 0.025ml of stannous chloride solution (Neas & Guyon, 1969). The mixture was incubated at 30°C for 30min.…”

Section: Thiocyanate Determinationmentioning

confidence: 99%

Turkey liver xanthine dehydrogenase. Reactivation of the cyanide-inactivated enzyme by sulphide and by selenide

Cleere

Coughlan

1974

Biochemical Journal

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1. Turkey liver xanthine dehydrogenase engaged in catalysing the oxidation of xanthine by dichlorophenol-indophenol was progressively inactivated by methanol. This inactivation was reversible by NAD(+). 2. Reaction with arsenite and with cyanide, in each case first-order with respect to enzyme, resulted in characteristic alterations in the visible absorption spectrum of the enzyme. The rate of spectral change on reaction with either agent paralleled the rate of loss of enzyme activity. 3. Cyanide inactivation was accompanied by elimination from the enzyme of sulphur as thiocyanate. Partial restoration of activity was effected by incubation with sulphide or with selenide. The results suggest that turkey liver xanthine dehydrogenase, like milk xanthine oxidase (Massey & Edmonson, 1970), contains at the active centre a cyanolysable persulphide group essential to catalytic activity and that selenium may replace sulphur in this group to give an active enzyme. 4. Incubation of the native enzyme with sulphide or with selenide resulted in the rapid loss of half of the xanthine-oxidizing activity, apparently by disrupting the molybdenum and (Fe/S)II loci. This may indicate non-equivalence of the intramolecular electron-transfer systems.

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Determination of thiocyanic acid in diisopropyl ester

Nazarova¹,

Golomazova²

1978

Fibre Chem

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Spectrophotometric determination of thiocyanate with rhenium

Cited by 8 publications

References 17 publications

Turkey liver xanthine dehydrogenase: properties of the enzyme dependent on the content of functional active sites (Short Communication)

Turkey liver xanthine dehydrogenase: properties of the enzyme dependent on the content of functional active sites (Short Communication)

Turkey liver xanthine dehydrogenase. Reactivation of the cyanide-inactivated enzyme by sulphide and by selenide

Determination of thiocyanic acid in diisopropyl ester

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