Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of <i>Ogataea parapolymorpha</i>.

ABSTRACT: Mitochondria from Ogataea parapolymorpha harbor a branched electron-transport chain containing a proton-pumping Complex I NADH dehydrogenase and three Type II NADH dehydrogenases (NDH-2). To investigate the physiological role, localization and substrate specificity of these enzymes, the growth of various NADH dehydrogenase knockout mutants was quantitatively characterized in shake-flask and chemostat cultures, followed by oxygen-uptake experiments with isolated mitochondria. NAD(P)H:quinone oxidoreduction of the three NDH-2 were individually assessed. Our findings reveal that the O. parapolymorpha respiratory chain contains an internal NADH-accepting NDH-2 (Ndh2-1/OpNdi1), at least one external NAD(P)H-accepting enzyme, and likely additional mechanisms for respiration-linked

SUBMITTER: Juergens H 

PROVIDER: S-EPMC11670749 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature