location of F1 particle of ATP synthase in thylakoid membrane is
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Located within the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of two regions FO and F1. FO causes rotation of F1 and is made of c-ring and subunits a, b, d, F6. F1 is made of {\displaystyle \alpha ,\beta ,\gamma ,\delta } subunits. F1 has a water-soluble par that can hydrolyze ATP. FO on the other hand has mainly hydrophobic regions. FO F1creates a pathway for protons movement across the membrane.[7]
F1 regio
The F1 portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. Subunits {\displaystyle \alpha } and {\displaystyle \beta } make a hexamer with 6 binding sites. Three of them are catalytically inactive and they bind ADP.
Other three subunits catalyze the ATP synthesis. The other F1 subunits {\displaystyle \gamma ,\delta ,\epsilon } are a part of a rotational motor mechanism. {\displaystyle \gamma }subunit allows {\displaystyle \beta } to go though conformational changes, i.e. closed, half open and open states allows for ATP to be bound and released once synthesized. The F1 particle is large and can be seen in the transmission electron microscope by negative staining.[8]These are particles of 9 nm diameter that pepper the inner mitochondrial membrane
F1 regio
The F1 portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. Subunits {\displaystyle \alpha } and {\displaystyle \beta } make a hexamer with 6 binding sites. Three of them are catalytically inactive and they bind ADP.
Other three subunits catalyze the ATP synthesis. The other F1 subunits {\displaystyle \gamma ,\delta ,\epsilon } are a part of a rotational motor mechanism. {\displaystyle \gamma }subunit allows {\displaystyle \beta } to go though conformational changes, i.e. closed, half open and open states allows for ATP to be bound and released once synthesized. The F1 particle is large and can be seen in the transmission electron microscope by negative staining.[8]These are particles of 9 nm diameter that pepper the inner mitochondrial membrane
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