1. Setting the Record Straight: A New Twist on the Chemiosmotic Mechanism of Oxidative Phosphorylation.
- Author
-
Juhaszova, Magdalena, Kobrinsky, Evgeny, Zorov, Dmitry B, Aon, Miguel A, Cortassa, Sonia, and Sollott, Steven J
- Subjects
- *
OXIDATIVE phosphorylation , *ADENOSINE triphosphatase , *BIOENERGETICS , *COMMODITY exchanges , *BIOLOGICAL interfaces - Abstract
It involves the I two i -ion I anti i port of K SP + sp with H SP + sp inside the ATP synthase molecule to make ATP, without a clear ability to develop significant, positively adaptive changes in osmotic drive (Fig. Under these latter conditions, these are pure K SP + sp currents (driven by pK), and when the vector of their charge movement is properly directed (with respect to the orientation of ATP synthase), they drive and enable ATP synthase to produce ATP. Importantly, without adding FCCP (to allow a H SP + sp leak pathway), there is no ATP synthesis in a K SP + sp gradient, so there must be no functional K/H exchange activity present inside ATP synthase such as is central to the proposed Nath mechanism. In stark contrast, Nath's "two-ion theory of energy coupling" model[15] proposes an electroneutral H SP + sp /K SP + sp I anti i port within the F SB 1 sb F SB o sb -ATP synthase itself to maintain electroneutrality[15] (Fig. [Extracted from the article]
- Published
- 2022
- Full Text
- View/download PDF