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Pyridine nucleotide transhydrogenations in yeast.

T C Evans, B Mackler, R Grace

Archives of Biochemistry and Biophysics

|December 1, 1985

Summary

Yeast extracts show significant pyridine nucleotide transhydrogenation activity, primarily in the cytosol. This study details the molecular forms and subcellular locations of this crucial enzymatic process in yeast.

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Area of Science:

Biochemistry
Molecular Biology
Yeast Metabolism

Background:

Pyridine nucleotide transhydrogenation is vital for cellular redox balance.
Previous studies indicated low or absent transhydrogenase activity in yeast.

Purpose of the Study:

To investigate and characterize pyridine nucleotide transhydrogenation activity in yeast.
To determine the subcellular localization and molecular forms of yeast transhydrogenase.

Main Methods:

Subcellular fractionation and differential centrifugation.
Sucrose density gradient centrifugation.
Enzyme activity assays at pH 8-9.
Spectroscopic analysis (UV fluorescence).

Main Results:

Significant transhydrogenase activity detected in yeast extracts at alkaline pH.
Cytosolic localization of high-molecular-weight transhydrogenase in Saccharomyces cerevisiae and Candida utilis.
Mitochondrial transhydrogenase activity solubilized from C. utilis, appearing in both high and low-molecular-weight forms.
Distinct fluorescence properties (salmon vs. yellow-green) associated with different molecular weight fractions.

Conclusions:

Yeast possesses significant pyridine nucleotide transhydrogenation activity, contrary to previous assumptions.
Multiple molecular forms of transhydrogenase exist in yeast, with distinct subcellular distributions.
Further research is needed to elucidate the precise roles and relationships of these yeast transhydrogenase forms to other metabolic pathways.

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