ATP Synthetase......................pptx

function
mechanism
structure
types
inhibitor

1. ATP Synthetase Tanvi N. Raulaji Department of Biosciences, Bakrol

2. . What is it Location Function Structure mechanism Who is Discovered Inhibitor Types

3. Paul Boyer proposed that ATP synthase is Cylinder with alternating alpha & beta Subunit. In 1960 the American scientist Efraim Racker and co workers isolated from mitochondria, the enzyme “F0 F1 ATPase” he was also told that ATP synthase is also called COMPLEX V John Walker used X-ray Crystallography to determine the structure of ATP Synthase.so. It’s give conformation of this boyer theory. . . .

4. What is ATP Synthase ATP synthase is an enzyme that produces adenosine Triphosphate(ATP) , the primary molecule that stores and transfers energy in biochemical reaction. In Oxidative Phosphorylation is carried out by five complexes, which are the sites for electron transport and ATP Synthesis. This Complex v is responsible for the generation of ATP through phosphorylation of ADP by using electrochemical energy generated by proton gradient across the inner membrane of mitochondria. Location In Prokaryotes Plasma Membrane In Eukaryotes Inner Mitochondrial Membrane 4

5. Why ATP Synthase is Called Energy Currency ? - The statement "ATP synthase is the energy currency of the cell" is incorrect. ATP (adenosine triphosphate) itself is the energy currency of the cell, not ATP synthase. Function of ATP Energy Carrier : ATP is a molecule that stores and transfers energy within cells. Energy Storage : The high-energy phosphate bonds between the phosphate groups that’s store significant amounts of energy. Energy Release : When ATP is broken down into ADP (adenosine diphosphate) and inorganic phosphate, this bond is broken, releasing energy that can be used for various cellular processes Energy Conversion : It is responsible for converting the potential energy stored in a proton gradient into chemical energy in the form of ATP. so, ATP: The energy currency of the cell. ATP Synthase: The enzyme that produces ATP using the energy from a proton gradient. Therefore, ATP synthase is not the energy currency itself, but rather the crucial enzyme that helps generate it.

6. CHEMIOSMOTIC THEORY The process of transfer the electron from NADH & FADH2 to o2 to series of electron carriers, thereby chemical energy in order to produce adenosine triphosphate(ATP). This all phenomenon is called Oxidative phosphorylation. This chemiosmotic theory is proposed by Peter Mitchell in 1961 ( Nobel prize, 1978) The transport of protons from inside to outside of inner mitochondrial membrane is accompanied by the generation of a proton gradient across the membrane, so Proton (H+ ions ) accumulate outside the membrane , creating an electrochemical potential difference. This proton motive force drives the synthesis of ATP by ATP synthase complex. .

7. Structure of Complex V 7 The structure of ATP synthase consists of two main protein components: the membrane-bound F  portion which is attached to the inner mitochondrial membrane and the water-soluble F 1  portion in the mitochondrial matrix. F0 Subunit F  region is embedded in the cell’s membrane & Hydrophobic portion composed of three subunits a, b, and c.  It’s acts as a proton channel , allowing the passage of protons across the membrane. This flow of proton provides the driving force for the rotation of F1 subunit , which ultimately leads to synthesis of ATP. there is a ring composed of 9-12 c-subunits, arranged in a circular way. This ring is tightly linked to one a-subunit and two b-subunits of F .  The a-subunit acts as a mediator for proton transfer between the c-ring and the surrounding environment outside the cell. F  is also bound to several other subunits within the F 1  region of the synthase. The F  and F 1  domains are connected by the peripheral stalk.

8. Mechanism of F0 Subunit Presentation Title 3 type of subunit occur a Subunit this are anchors the F 0 subunit to membrane and interact with F1 subunit. b Subunit these form a proton channel through the membrane.{as stalk} c Subunit these are rotate as proton pass through the channel, driving the rotation of the Gamma subunit in F1. {Act as Rotor ring} PROTON TRANSLOCATION Proton binding : protons bind to the c subunit at a specific site. Rotation : the binding of proton cause a conformational change in the c subunit , leadind to their rotation with in membrane. Proton Release : the c subunit, they release the proton into the matrix. In short, F0 subunit play role in converting the potential energy stored in the proton gradient into Rotational energy, which is then used by F1 subunit to synthesize ATP.

9. Mechanism of F1 Subunit Presentation Title The F0 subunit is the hydrophilic portion of ATP synthase located in mitochondrial matrix. It is responsible for the actual synthesis of ATP, utilizing the energy derived from rotation of the F0 subunit. There are 4 type of subunit occur Alpha subunit it’s bind ADP & Inorganic Phosphate(Pi) to form ATP. beta Subunit it’s catalyze the synthesis of ATP from ADP & Pi . There are three beta subunit , Each in a different conformational state: Loose State Here binding site for ADP + pI Beta Subunit Tight state here catalyzes formation of ATP. . Open state here release the newly synthesized ATP Gamma Subunit this subunit rotates as protons flow through the F0 subunit, driving the conformational changes in alpha & beta subunit that lead to ATP synthesis. Epsilon Subunit it’s stabilizes the Gamma subunit and prevent its uncontrolled rotation.

10. Presentation Title 10

11. . Presentation Title

12. Presentation Title through a-subunit proton transfer between the c-ring and the surrounding environment Proton binds to C subunit & Rotational activity is start B subunit act a proton channel Proton (H+) ions flow through F0 subunit Alpha & Beta undergo Conformational change When beta in loose stage, bind ADP + Pi in Tight stage, formation of ATP in open stage, release of ATP Molecule 12 Pathway

13. Animation Presentation Title

14. Inhibitor Of Complex v  Oligomycin A It’s binds to F0 subunit & then inhibiting flow of proton through the channel . this prevent Rotation of F1 Subunit. DNP It’s uncoupler that disrupts proton gradient across inner mitochondrial membrane. so PMF is dissipate. CCCP Uncoupler Dissipates proton Gradient by increasing the permeability of inner mitochondrial membrane to proton. Aurovertin It’s binds to the beta subunit of F1 Subunit so inhibiting ATP Synthesis. Bafilomycin Concanamycin this both are antibiotic which is inhibit this complex through Reducing ATP production 14 It’s inhibited by prevent conversion of cytochrome c Oxidase , which is component of ETC . this prevents the cell from using oxygen , which can lead to histotoxic anoxia. Cyanide

15. . Presentation Title Types Example Location Inhibitor P type [Phosphorylation Type] Na+ K+ ATPase Ca+2 pump Plasma membrane Oligomycin DCCD V type [Vacuolar Type] H+ K+ ATPase Vacuoles Lysosomes Endosomes Bafilomycin Concanamycin F type [Energy coupling Factor] ATP synthase Mitochondria Plasma membrane Oligomycin

16. g Presentation Title Na+/ k+ pump

17. Presentation Title

18. V Type Presentation Title

19. Page no 704-715 Reference Books

20. Page No: 543-549

21. Types of ATP synthase

22. Where is located of Complex V Prokaryotes & Eukaryotes ? Which is the Catalytic part of ATP Synthase? Give any two inhibitors name : How many types of ATPase ? How many proton required for formation of 5 ATP??? Presentation Title Formation Required 1 ATP 4 proton 5 ATP (?) 5*4 20 ATP

23. Thank You Presentation Title