The mechanism of the cyanide inhibition of fermentation

Meyerhof, Otto; Kaplan, Ann E.

doi:10.1016/0003-9861(52)90199-9

Cited by 8 publications

(2 citation statements)

References 10 publications

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“…The possibility cannot be excluded, however, that cyanide may also inhibit the DPNor TPN-dependent hydroxysteroid dehydrogenases (cf. Meyerhof and Kaplan, 1952). Thus the quantitative significance of the rates in Table IV should Androstan-3a-ol-17-one 0.054 0.018 0.026 0.056 " Incubated with DPN or TPN and fresh microsomal fraction at pH 9.6, based on the increase in absorbancy (+ A A) due to formation of DPNH or TPNH (wavelength = 340 ium, <7 = 1 cm).…”

Section: Resultsmentioning

confidence: 98%

Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver^*

Repke¹,

Samuels²

1964

Biochemistry

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Section: Resultsmentioning

confidence: 98%

Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver^*

Repke¹,

Samuels²

1964

Biochemistry

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“…The oxidation of DPNH in the presence of mitochondria and substrate was sensitive to inhibitors such as antimycin and cyanide. Cyanide, however, was not a suitable inhibitor in these studies due to its reaction with metmyoglobin (31) as well as with DPN and flavoproteins (32). The effect of metmyoglobin in partially reversing the inhibition of DPNH oxidation due to antimycin can be seen in Table I.…”

Section: Reduction Of Ferrylmyoglobin By Dpnhmentioning

confidence: 96%

Metmyoglobin Oxidation during Electron Transport Reactions in Mitochondria

Kaplan-Bresler

1965

The Journal of General Physiology

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Studies of the intracellular role of myoglobin were carried out by recording spectrophotometric changes in acid metmyoglobin and oxymyoglobin during electron transport reactions with mitochondria prepared from pigeon heart muscle by the method of Chance and Hagihara. The absorption peak of metmyoglobin at 409 m/s disappeared when substrate was added to normal or antimycin-inhibited preparations, and was replaced by a new maximum at 423 to 424 my, identified as due to the oxidation to ferrylmyoglobin. Further investigation revealed that the oxidation of metmyoglobin took place with the simultaneous oxidation of reduced flavoprotein. Hydrogen peroxide, formed by the reaction of reduced flavoprotein with oxygen, was considered to be the probable intermediate for the oxidation of metmyoglobin in experiments in which catalase was added as a competitor for the oxidant. When DPNH was added to the reaction mixture, the reductant acted to resynthesize the ferri-derivative by reaction with ferrylmyoglobin. Oxymyoglobin could not be used in place of metmyoglobin in these systems. Under the experimental conditions, oxymyoglobin dissociated when dissolved oxygen was depleted from the medium by enzyme oxidations; the resultant ferromyoglobin underwent oxidation to metmyoglobin.

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Über die Wirkung einiger Enzymgifte auf die Citronensäuregärung nach dem Oberflächenverfahren

Leopold¹

1959

Nahrung

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The mechanism of the cyanide inhibition of fermentation

Cited by 8 publications

References 10 publications

Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver^*

Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver^*

Metmyoglobin Oxidation during Electron Transport Reactions in Mitochondria

Über die Wirkung einiger Enzymgifte auf die Citronensäuregärung nach dem Oberflächenverfahren

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The mechanism of the cyanide inhibition of fermentation

Cited by 8 publications

References 10 publications

Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver*

Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver*

Metmyoglobin Oxidation during Electron Transport Reactions in Mitochondria

Über die Wirkung einiger Enzymgifte auf die Citronensäuregärung nach dem Oberflächenverfahren

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Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver^*

Enzymatic Basis for Epimerization of Cardiotonic Steroids at Carbon 3 in Rat Liver^*