Titre du document / Document title

Activation and inhibition of mitochondrial transhydrogenase by metal ions

Auteur(s) / Author(s)

SAZANOV L. A. ; JACKSON J. B. ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

Univ. Birmingham, school biochemistry, Birmingham B15 2TT, ROYAUME-UNI

Résumé / Abstract

Mitochondrial transhydrogenase has been reported previously to be inhibited by high, rather non-physiological concentrations (in the range of 2-20 mM) of divalent cations. We show that the enzyme could be activated by low (from about 1 μM to 1 mM) concentrations of Ca²⁺ and Mg²⁺, which are within physiological range. These results bring in line the effects observed with mitochondrial enzyme to the findings with bacterial transhydrogenases. The activation of transhydrogenase by divalent cations is interpreted as an increase in affinity of the NADP(H)-binding site of the enzyme-NAD(H) complex. Reported effects of the metal ions could be important for the enzyme function in vivo

Revue / Journal Title

Biochimica et biophysica acta. Bioenergetics   ISSN 0005-2728 

Source / Source

1993, vol. 1144, n^o2, pp. 225-228 (19 ref.)

Langue / Language

Anglais

Editeur / Publisher

Elsevier, Amsterdam, PAYS-BAS  (1967) (Revue)

Mots-clés anglais / English Keywords

Mitochondria ; NAD(P)+ transhydrogenase ; Enzymatic activity ; Metal ion ; Heart ; Bovine ; Enzyme ; Artiodactyla ; Ungulata ; Mammalia ; Vertebrata ;

Mots-clés français / French Keywords

Mitochondrie ; NAD(P)+ transhydrogenase ; Activité enzymatique ; Ion métallique ; Coeur ; Bovin ; Enzyme ; Artiodactyla ; Ungulata ; Mammalia ; Vertebrata ;

Mots-clés espagnols / Spanish Keywords

Mitocondria ; NAD(P)+ transhydrogenase ; Actividad enzimática ; Ión metálico ; Corazón ; Bovino ; Enzima ; Artiodactyla ; Ungulata ; Mammalia ; Vertebrata ;

Localisation / Location

INIST-CNRS, Cote INIST : 3973 A, 35400004754363.0140