Redox control of hydrogenase activity in the green alga Scenedesmus obliquus by thioredoxin and other thiols.
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 (I50 = 21 nM) and E. coli thioredoxin (I50 = 83 nM). For the homologous cytoplasmic thioredoxins I+II an I50 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.
Wünschiers
R
R
Fachbereich Biologie/Botanik, Philipps-Universität, Marburg, Germany.
Heide
H
H
Follmann
H
H
Senger
H
H
Schulz
R
R
D000460:Chlorophyta / Q000201:enzymology*; D004926:Escherichia coli / Q000378:metabolism; D006864:Hydrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D013438:Sulfhydryl Compounds / Q000494:pharmacology*; D013879:Thioredoxins / Q000494:pharmacology*
D013438:Sulfhydryl Compounds; D013879:Thioredoxins; C043296:nickel-iron hydrogenase; D006864:Hydrogenase