An increasingly important area of research is based on sulphydryl chemistry, since the oxidation of -SH groups is one of the earliest observable events during oxidant-mediated damage and -SH groups play a critical role in the function of many macromolecular structures including enzymes, transcription factors and membrane proteins. Glutaredoxins and thioredoxins are small heat-stable oxidoreductases, conserved throughout evolution, which play key roles in maintaining the cellular redox balance. Much progress has been made in analysing these systems in the yeast Saccharomyces cerevisiae which is a very useful model eukaryote due to its ease of genetic manipulation, its compact genome, the availability of the entire genome sequence, and the current rate of progress in gene function research. Yeast, like all eukaryotes, contains a number of glutaredoxin and thioredoxin isoenzymes located in both the cytoplasm and the mitochondria. This review describes recent findings made in yeast that are leading to a better understanding of the regulation and role of redox homeostasis in eukaryotic cell metabolism.