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Redox control of hydrogenase activity in the green alga Scenedesmus obliquus by thioredoxin and other thiols
Author(s) -
Wünschiers Röbbe,
Heide Heinrich,
Follmann Hartmut,
Senger Horst,
Schulz Rüdiger
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00867-4
Subject(s) - thioredoxin , dithiothreitol , hydrogenase , biochemistry , dehydrogenase , glutathione , enzyme , glutaredoxin , thioredoxin reductase , biology , chemistry
The activity of the NiFe‐hydrogenase from the green alga Scenedesmus obliquus is inhibited by both algal thioredoxins f and I+II, and by Escherichia coli thioredoxin. The strongest inhibition was observed with homologous chloroplastic thioredoxin f (I 50 =21 nM) and E. coli thioredoxin (I 50 =83 nM). For the homologous cytoplasmic thioredoxins I+II an I 50 of 667 nM was determined. Glutathione shows a similar but much less pronounced inhibitory effect whereas dithiothreitol had no effect. In addition to glucose‐6‐phosphate dehydrogenase, NiFe‐hydrogenase is only the second enzyme known to be inhibited by reduced thioredoxin.