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

Volumn 255, Issue 1, 1998, Pages 185-195

  Krimm, I ^a   Lemaire, S ^a   Ruelland, E ^a   Miginiac Maslow, M ^a   Jaquot, J P ^a   Hirasawa, M ^a   Knaff, D B ^a   Lancelin, J M ^a  

^a UNIVERSITÉ LYON 1   (France)

Author keywords

Chlamydomonas reinhardtii; Cysteine pK(a); NMR; Redox potential; Theoredoxin h

Indexed keywords

CYSTEINE; THIOREDOXIN;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CHLAMYDOMONAS REINHARDTII; MUTATION; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

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; POTENTIOMETRY; RECOMBINANT PROTEINS; THIOREDOXIN; TRYPTOPHAN;

ALGAE; CHLAMYDOMONAS REINHARDTII; ESCHERICHIA COLI; EUKARYOTA;

EID: 0032125811     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550185.x     Document Type: Article

References (59)