Abstract:
:The mitochondrial flavoenzyme l-galactono-gamma-lactone dehydrogenase (GALDH) catalyzes the ultimate step of vitamin C biosynthesis in plants. We found that recombinant GALDH from Arabidopsis (Arabidopsis thaliana) is inactivated by hydrogen peroxide due to selective oxidation of cysteine (Cys)-340, located in the cap domain. Electrospray ionization mass spectrometry revealed that the partial reversible oxidative modification of Cys-340 involves the sequential formation of sulfenic, sulfinic, and sulfonic acid states. S-Glutathionylation of the sulfenic acid switches off GALDH activity and protects the enzyme against oxidative damage in vitro. C340A and C340S GALDH variants are insensitive toward thiol oxidation, but exhibit a poor affinity for l-galactono-1,4-lactone. Cys-340 is buried beneath the protein surface and its estimated pK(a) of 6.5 suggests the involvement of the thiolate anion in substrate recognition. The indispensability of a redox-sensitive thiol provides a rationale why GALDH was designed as a dehydrogenase and not, like related aldonolactone oxidoreductases, as an oxidase.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Leferink NG,van Duijn E,Barendregt A,Heck AJ,van Berkel WJdoi
10.1104/pp.109.136929subject
Has Abstractpub_date
2009-06-01 00:00:00pages
596-605issue
2eissn
0032-0889issn
1532-2548pii
pp.109.136929journal_volume
150pub_type
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