Hydroperoxides (H2O2 and ROOH) are damaging in living cells because they give rise to the raidicals OH’ and RO’. The cellular machinery is equipped to limit the accumulation of hydroperoxides. This control is primarily achieved by a variety of peroxidases which reduce ROOH to ROH and H2O. This review describes two recently identified peroxidases, thioredoxin peroxidase (TPx) and alkyl hydroperoxidase (AhpC). TPx and AhpC are similar in amino acid sequence and define a family (named the peroxiredoxin family) of more than 26 different proteins which are present in organisms from all kingdoms, but have not been associated with known biochemical functions. All members of the peroxiredoxin family contain one conserved cysteine, which appears to be the primary site of reaction with hydroperoxide. The diversity in the amino acid sequences of the family members in part reflects different mechanisms involved in the regeneration of reduced peroxiredoxin.
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Rhee et al. (1994) studied this question.
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