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. 1978 Apr;61(4):601–605. doi: 10.1104/pp.61.4.601

Light Modulation of Enzyme Activity

Activation of the Light Effect Mediators by Reduction and Modulation of Enzyme Activity by Thiol-Disulfide Exchange 1

Louise E Anderson 1, Sooja C Nehrlich 1, Marie-Louise Champigny 1,2
PMCID: PMC1091926  PMID: 16660345

Abstract

Light and dark modulation experiments with pea (Pisum sativum L.) chloroplast stromal fractions pretreated with dithiothreitol (to reduce protein disulfide bonds) or with 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB) (to block sulfhydryl groups) suggest that light modulation involves thiol-disulfide exchange on the modulatable stromal enzyme protein. Light-dependent reduction of DTNB involves a photosynthetic electron transport chain component located on the reducing side of photosystem I prior to ferredoxin; DTNB may be acting as a light effect mediator substitute. The thylakoid-bound light effect mediator system, then, in its light-activated reduced form probably catalyzes thiol-disulfide exchange reactions on stromal enzymes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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