1932

Abstract

Initially discovered in the context of photosynthesis, regulation by change in the redox state of thiol groups (S−S ↔ 2SH) is now known to occur throughout biology. Several systems, each linking a hydrogen donor to an intermediary disulfide protein, act to effect changes that alter the activity of target proteins: the ferredoxin/thioredoxina small protein, reduced enzymatically by NADPH or ferredoxin, that is active in thiol/disulfide exchange and results in regulation or substrate conversion system, comprised of reduced ferredoxin, a thioredoxin, and the enzyme, ferredoxin-thioredoxin reductase; the NADP/thioredoxin system, including NADPH, a thioredoxin, and NADP-thioredoxin reductase; and the glutathione/glutaredoxina small protein, reduced by glutathione, that is active in thiol/disulfide exchange and results in regulation or substrate conversion system, composed of reduced glutathione and a glutaredoxin. A related disulfide protein, protein disulfide isomerase (PDI) acts in protein assembly. Regulation linked to plastoquinone and signaling induced by reactive oxygen species (ROSreactive oxygen species ) and other agents are also being actively investigated. Progress made on these systems has linked redox to the regulation of an increasing number of processes not only in plants, but in other types of organisms as well. Research in areas currently under exploration promises to provide a fuller understanding of the role redox plays in cellular processes, and to further the application of this knowledge to technology and medicine.

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/content/journals/10.1146/annurev.arplant.56.032604.144246
2005-06-06
2024-04-13
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  • Article Type: Review Article
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