We present an update on the structure and function of ATP synthases, the ubiquitous enzymes of energy conservation. Although the focus of the chapter is on F1FO ATP synthase, we will first illustrate the structural features of the simpler bacterial enzyme. This should allow a better understanding of the additional features conferred to F1FO ATP synthases by unique subunits that are not essential for ATP synthesis. These “accessory” subunits mediate interactions between enzyme monomers in mitochondria resulting in the formation of dimers and then of long rows of oligomers located in the depth of the cristae, which they critically contribute to form. An emerging function of mitochondrial ATP synthase is the Ca2+-dependent formation of a high-conductance channel, the permeability transition pore (PTP). We will cover the features of this channel and potential mechanisms through which ATP synthase is turned from an energy-conserving into an energy-dissipating system.
ATP synthase: Structure, function, and channel formation
Lippe G.;Fogolari F.;
2025-01-01
Abstract
We present an update on the structure and function of ATP synthases, the ubiquitous enzymes of energy conservation. Although the focus of the chapter is on F1FO ATP synthase, we will first illustrate the structural features of the simpler bacterial enzyme. This should allow a better understanding of the additional features conferred to F1FO ATP synthases by unique subunits that are not essential for ATP synthesis. These “accessory” subunits mediate interactions between enzyme monomers in mitochondria resulting in the formation of dimers and then of long rows of oligomers located in the depth of the cristae, which they critically contribute to form. An emerging function of mitochondrial ATP synthase is the Ca2+-dependent formation of a high-conductance channel, the permeability transition pore (PTP). We will cover the features of this channel and potential mechanisms through which ATP synthase is turned from an energy-conserving into an energy-dissipating system.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
