Aufsatz in einer Fachzeitschrift
Organelle-specific NADPH thioredoxin reductase in plant mitochondria
Details zur Publikation
Autor(inn)en: | Banze, M.; Follmann, H. |
Publikationsjahr: | 2000 |
Zeitschrift: | Journal of Plant Physiology |
Seitenbereich: | 126-129 |
Jahrgang/Band : | 156 |
ISSN: | 0176-1617 |
Zusammenfassung, Abstract
Plant mitochondria contain one or two specific mt-thioredoxins which participate, inter alia, in the regulation of the ketoglutarate dehydrogenase complex. The presence of thioredoxin reductase, second component of a typical thioredoxin system inside mitochondria has, however, remained uncertain. We here show that potato tuber mitochondrial lysates contain an enzyme of 40 kDa monomer mass, utilizing NADPH and plant (but not bacterial) thioredoxins as substrates, It is distinct From a 35 kDa reductase of cytosolic origin. Plants thus contain a third thioredoxin reductase, mt-NTR, in addition to the known NTR and ferredoxin-dependent FTR enzyme.
Plant mitochondria contain one or two specific mt-thioredoxins which participate, inter alia, in the regulation of the ketoglutarate dehydrogenase complex. The presence of thioredoxin reductase, second component of a typical thioredoxin system inside mitochondria has, however, remained uncertain. We here show that potato tuber mitochondrial lysates contain an enzyme of 40 kDa monomer mass, utilizing NADPH and plant (but not bacterial) thioredoxins as substrates, It is distinct From a 35 kDa reductase of cytosolic origin. Plants thus contain a third thioredoxin reductase, mt-NTR, in addition to the known NTR and ferredoxin-dependent FTR enzyme.
