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| Content Provider | Directory of Open Access Journals (DOAJ) |
|---|---|
| Author | Mohamed eKaramoko Stéphane eGabilly Patrice Paul Hamel |
| Abstract | Thiol oxidation to disulfides and the reverse reaction, i.e. disulfide reduction to free thiols, are under the control of catalysts in vivo. Enzymatically assisted thiol-disulfide chemistry is required for the biogenesis of all energy-transducing membrane systems. However, until recently, this had only been demonstrated for the bacterial plasma membrane. Long considered to be vacant, the thylakoid lumen has now moved to the forefront of photosynthesis research with the realization that its proteome is far more complicated than initially anticipated. Several lumenal proteins are known to be disulfide bonded in Arabidopsis, highlighting the importance of sulfhydryl oxidation in the thylakoid lumen. While disulfide reduction in the plastid stroma is known to activate several enzymatic activities, it appears that it is the reverse reaction, i.e. thiol oxidation that is required for the activity of several lumen-resident proteins. This paradigm for redox regulation in the thylakoid lumen has opened a new frontier for research in the field of photosynthesis. Of particular significance in this context is the discovery of trans-thylakoid redox pathways controlling disulfide bond formation and reduction, which are required for photosynthesis. |
| e-ISSN | 1664462X |
| DOI | 10.3389/fpls.2013.00476 |
| Journal | Frontiers in Plant Science |
| Volume Number | 4 |
| Language | English |
| Publisher | Frontiers Media S.A. |
| Publisher Date | 2013-11-01 |
| Publisher Place | Switzerland |
| Access Restriction | Open |
| Subject Keyword | Plant Culture Cytochrome B6f Complex Photosynthesis Photosystem Ii Protein Complex Thylakoid Lumen Thiol Based Chemistry |
| Content Type | Text |
| Resource Type | Article |
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