ND3, ND1 and 39kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I.

ABSTRACT: An intriguing feature of mitochondrial complex I from several species is the so-called A/D transition, whereby the idle enzyme spontaneously converts from the active (A) form to the de-active (D) form. The A/D transition plays an important role in tissue response to the lack of oxygen and hypoxic deactivation of the enzyme is one of the key regulatory events that occur in mitochondria during ischaemia. We demonstrate for the first time that the A/D conformational change of complex I does not affect the macromolecular organisation of supercomplexes in vitro as revealed by two types of native electrophoresis. Cysteine 39 of the mitochondrially-encoded ND3 subunit is known to become exposed upon de-activation. Here we show that even if complex I is a constituent of the I+III2+IV (S1) supercom

SUBMITTER: Babot M 

PROVIDER: S-EPMC4331043 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature