Effect of monovalent cations on the kinetics of hypoxic conformational change of mitochondrial complex I.

ABSTRACT: Mitochondrial complex I is a large, membrane-bound enzyme central to energy metabolism, and its dysfunction is implicated in cardiovascular and neurodegenerative diseases. An interesting feature of mammalian complex I is the so-called A/D transition, when the idle enzyme spontaneously converts from the active (A) to the de-active, dormant (D) form. The A/D transition plays an important role in tissue response to ischemia and rate of the conversion can be a crucial factor determining outcome of ischemia/reperfusion. Here, we describe the effects of alkali cations on the rate of the D-to-A transition to define whether A/D conversion may be regulated by sodium. At neutral pH (7-7.5) sodium resulted in a clear increase of rates of activation (D-to-A conversion) while other cations had minor ef

SUBMITTER: Stepanova A 

PROVIDER: S-EPMC4607728 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature