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ATP Synthase

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ATP Synthase- enzyme that catalyses ATP synthesis and hydrolysis ... http://www.stolaf.edu/people/giannini/flashanimat/metabolism/atpsyn1.swf ... – PowerPoint PPT presentation

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Title: ATP Synthase


1
ATP Synthase
  • Final Model Project
  • By Jerry, Michael and Lisa

2
What is ATP Synthase?
  • ATP (adenosine triphosphate) the molecule of
    energy for cells, drives many biochemical
    reactions like muscle contraction, DNA and
    protein synthesis, etc
  • ATP Synthase- enzyme that catalyses ATP synthesis
    and hydrolysis

http//users.rcn.com/jkimball.ma.ultranet/BiologyP
ages/A/ATP.html
3
Where is it found?
  • A membrane enzyme
  • Found in
  • bacterial plasma membranes
  • The thylacoid membrane in chloroplasts
  • The inner mitochondrial membrane of eukaryotic
    cells

http//www.biologie.uni-osnabrueck.de/biophysik/Fe
niouk/images/Rb_capsulatus.jpg
4
Parts of ATP Synthase
  • Consists of two domains F0 and F1

http//www.sigmaaldrich.com/Area_of_Interest/Bioch
emicals/Enzyme_Explorer/Key_Resources/Metabolic_Pa
thways/ATP_Synthase.html
5
The Domains
  • Hydrophobic F0 domain sits in the membrane -
    performs proton translocation
  • Hydrophillic F1 portion protrudes from membrane -
    performs ATP synthesis/hydrolysis
  • 3 alternating alpha
  • and beta subunits

http//nobelprize.org/chemistry/laureates/1997/ill
pres/boyer-walker.html
6
What does it do?
  • It makes ATP from ADP and inorganic phosphate
    (Pi)
  • ADP Pi
    ATP
  • The overall equation is
  •     ADP3- HPO42- H nHoutside membrane(
    charge)  
  •   ATP4- H2O nHinside membrane
    (- charge)

energy from protons diffusing across membrane
with the gradient
7
How does it function?
  • First a proton gradient is established
  • Protons collect on one side of the membrane
  • Then the protons flow through a channel in the
    enzyme causing the protein subunits to rotate

http//www.sp.uconn.edu/terry/images/anim/ATPmito
.html
8
  • The stalk rotates in 120 increments
  • causes the units in the F1 domain to contract
    and expand
  • The structural changes facilitate the binding of
    ADP and Pi to make ATP
  • Each subunit goes through 3 stages
  • Open State releases any ATP
  • Loose State ADP and Pi molecules enter the
    subunit
  • Tight State the subunit contracts to bind
    molecules and make ATP

9
Animations
  • http//www.stolaf.edu/people/giannini/flashanimat/
    metabolism/atpsyn1.swf
  • Protons cross membrane through the ATP synthase
    enzyme
  • http//www.stolaf.edu/people/giannini/flashanimat/
    metabolism/atpsyn2.swf
  • Rotary motion of ATP synthase powers the
    synthesis of ATP

10
Video
http//nature.berkeley.edu/hongwang/Project/ATP_s
ynthase/
11
Interesting Facts
  • Contains 22722 atoms
  • 23211 bonds connected as 2987 amino acid groups
  • 120 helix units and 94 sheet units
  • Generates over 100 kg of ATP daily (in humans)
  • One of the oldest enzymes-appeared earlier then
    photosynthetic or respiratory enzymes
  • Smallest rotary machine known
  • Picture http//webct.uga.edu/public/FRES1010CG/BCM
    B401098ATPSyn2.gif/

12
Our Model
13
Sources for the PowerPoint
  • (http//www.biologie.uni-osnabrueck.de/biophysik/F
    eniouk/Basics.html),
  • (http//www.3dchem.com/molecules.asp?ID91),(http
    //www.biologie.uni-osnabrueck.de/biophysik/Feniou
    k/Basics.html)
  • http//www.sp.uconn.edu/terry/images/anim/ATPmito
    .html
  • http//www.mrc-dunn.cam.ac.uk/research/atpase.html
  • http//www.wiley.com/college/pratt/0471393878/stud
    ent/structure/atp_synthase/mechanism.html
  • http//rsb.info.nih.gov/NeuroChem/biomach/ATPsyn.h
    tml
  • http//webct.uga.edu/public/FRES1010CG/BCMB401098A
    TPSyn2.gif
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