Article
The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
European journal of biochemistry - 1 Jul 1998
Krimm I, Lemaire S, Ruelland E, Miginiac-Maslow M, Jaquot J P, Hirasawa M, Knaff D B, Lancelin J M
Abstract excerpt
The role of the invariant Trp residue at the redox site of thioredoxins was investigated by site-directed mutagenesis of a Chlamydomonas reinhardtii thioredoxin h. Though being still redox active with NADPH-thioredoxin reductase and chemical substrates [dithiothreitol and 5,5'-dithio-bis(2-nitrob...
Topics
- Animals
- Binding Sites
- Carbon Isotopes
- Chlamydomonas reinhardtii
- Hydrogen
- Hydrogen-Ion Concentration
- Malate Dehydrogenase
- Malate Dehydrogenase (NADP+)
- Models, Molecular
- Mutation
- Nuclear Magnetic Resonance, Biomolecular
- Oxidation-Reduction
- Plant Proteins