Sulphite reductase from bakers' yeast: A haemoflavoprotein

Prabhakararao, K.; Nicholas, D. J. D.

doi:10.1016/0005-2728(69)90112-1

Cited by 32 publications

(16 citation statements)

References 39 publications

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“…An NADPH-linked sulphite reductase activity has been demonstrated in a variety of strains of the yeast Succharotnyces cerevisiae by several groups using essentially the same methodology (de Vito and Dreyfuss 1964;Okuda and Uemura 1965;Yoshimoto and Sato 1968a;Prabhakararao and Nicholas 1969;Cherest et al 1971;Dott and Truper 1978;Stratford and Rose 1985). Initial efforts to demonstrate this activity in extracts of the wine yeast AWRI 77 were unsuccessful.…”

Section: Detection Of Nadph-linked Sulphite Reductase Activity In Yeamentioning

confidence: 99%

Determination of sulphite reductase activity and its response to assimilable nitrogen status in a commercial Saccharomyces cerevisiae wine yeast

Jiranek

Langridge

Henschke

1996

Journal of Applied Bacteriology

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The liberation of H2S is a common problem afflicting wine fermentation. Sulphite reductase activity of a commercial wine yeast was investigated to define its involvement in this process. The activity studied here differed from those characterized previously from cider and bakers' yeasts by displaying a greater sensitivity to cold, low ionic strength and possibly, proteolytic action. These differences necessitated the development of a new method of quantification. Through this method, the onset of H2S liberation was shown not to be a result of variations in the levels of sulphite reductase activity. Thus, high levels of activity which occurred during the exponential phase of growth were not necessarily accompanied by the liberation of H2S. Similarly, nitrogen-starved cultures which liberated H2S showed no corresponding increase in sulphite reductase activity from prestarvation levels. In fact, rates of H2S liberation from cultures and in enzyme assays agreed closely. A short-term independence of sulphite reductase activity from culture nitrogen status was therefore evident. The only influence of nitrogen was achieved in its absence when enzyme activity decayed with a half-life (4.25 h) which was comparable to that induced by the presence of cycloheximide (5.75 h). A proposed transcriptional control mechanism mediated by methionine derivatives was only partly effective in this strain although an in vitro inhibitory effect of methionine was implicated. These data therefore support the notion that H2S liberation in response to nitrogen starvation stems from a failure of metabolism to sequester H2S which continues to be formed, at least initially, at prestarvation rates.

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Section: Detection Of Nadph-linked Sulphite Reductase Activity In Yeamentioning

confidence: 99%

Determination of sulphite reductase activity and its response to assimilable nitrogen status in a commercial Saccharomyces cerevisiae wine yeast

Jiranek

Langridge

Henschke

1996

Journal of Applied Bacteriology

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“…The precise details of this six-electron-reduction process of sulfur are not understood and no free intermediates have been detected. The enzyme has been highly purified from yeast (26,27), higher plants (28), and Aspergillus nidulans (29), and in all cases it is a protein of high molecular weight containing a variety of bound cofactors. Among these are flavins, nonheme iron, sulfhydryl groups, and hemoprotein moieties, which suggest that sulfite reductase is in reality a multienzyme complex.…”

Section: Mechanism Of Selenate Transport and Metabolismmentioning

confidence: 99%

Selenium Biochemistry

Stadtman

1974

Science

320

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The toxicity of selenium to animals and plants has been known and extensively documented since the 1930's, but it is only during the past 15 years that selenium has also been shown to be an essential micronutrient for animals and bacteria. Very little is known about the specific role or roles of selenium and, to date, there are only three enzyme-catalyzed reactions that have been shown to require the participation of a selenium-containing protein. These are the reactions catalyzed by (i) formate dehydrogenase of bacteria, (ii) glycine reductase of clostridia, and (iii) glutathione peroxidase of erythrocytes. The common denominator of these selenium-dependent processes is that they are all oxidation-reduction reactions. A fourth selenoprotein has been isolated from skeletal muscle of sheep but its catalytic function has not been identified. The form in which selenium occurs in these selenoproteins is unknown. The selenoprotein of clostridial glycine reductase contains selenium in a covalently bound form. Studies in progress indicate that this may be an organoselenium compound not previously detected in nature. Identification of the chemical nature of selenium in proteins participating in electron transport processes should enable us to determine its specific role and to understand the basic defects in certain cardiac and skeletal muscle degenerative diseases which are selenium-deficiency syndromes. The greater availability and ease of isolation of the selenoprotein of the bacterial glycine reductase system makes this the biological material of choice for studies on the mechanism of action of selenium. An added attractive feature of this system is that it can conserve the energy made available by the reductive deamination of glycine in a biologically useful form by synthesizing ATP.

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“…7 The sulfite reductase was purified as described by Kobayashi and Yoshimoto. 4 Cyanogen bromide cleavage of the sulfite reductase a subunit was performed according to the procedure of Gross.…”

Section: Assay Of Sulfite Reductase Activity Purification Ofmentioning

confidence: 99%

Cloning and Sequencing of Sulfite Reductase Subunit Gene from Saccharomyces cerevisiae

et al. 1995

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A DNA fragment of 2.1 kb was specifically amplified by PCR with primers based on the amino acid sequences obtained from the N-terminal region and the cyanogen bromide-derived peptide of the sulfite reductase a subunit in Saccharomyces cerevisiae. With this fragment as a probe, the gene coding for the sulfite reductase a subunit was isolated from a genomic library of S. cerevisiae. Sequencing analysis revealed that the gene contains a 3105-bp open reading frame, which is large enough to code for a protein of 1035 amino acid residues. The transcript of the sulfite reductase a subunit gene was detected by Northern analysis after methionine deprevation, but the amount of the transcript did not directly correlate with the enzyme activity. The DNA fragment containing the sulfite reductase a subunit gene rescued the metlO phenotype by complementation.

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Sulphite reductase from bakers' yeast: A haemoflavoprotein

Cited by 32 publications

References 39 publications

Determination of sulphite reductase activity and its response to assimilable nitrogen status in a commercial Saccharomyces cerevisiae wine yeast

Determination of sulphite reductase activity and its response to assimilable nitrogen status in a commercial Saccharomyces cerevisiae wine yeast

Selenium Biochemistry

Cloning and Sequencing of Sulfite Reductase Subunit Gene from Saccharomyces cerevisiae

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