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    Lecture 1 ATP

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    maddie.jng
    ATP is the universal energy currency in biological systems. It is produced primarily through oxidative phosphorylation in the mitochondria, where a proton gradient is used by ATP synthase to catalyze the formation of ATP from ADP and inorganic phosphate. ATP is then utilized throughout the cell and hydrolyzed to drive various energy-requiring processes like biosynthesis, active transport, muscle contraction and nerve impulse transmission. The ATP-ADP cycle allows for the efficient regeneration and reuse of ATP through substrate-level phosphorylation and oxidative phosphorylation, meeting the large daily energy demands of organisms.

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    Lecture 1 ATP

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    maddie.jng
    13 views27 pages
    ATP is the universal energy currency in biological systems. It is produced primarily through oxidative phosphorylation in the mitochondria, where a proton gradient is used by ATP synthase to catalyze the formation of ATP from ADP and inorganic phosphate. ATP is then utilized throughout the cell and hydrolyzed to drive various energy-requiring processes like biosynthesis, active transport, muscle contraction and nerve impulse transmission. The ATP-ADP cycle allows for the efficient regeneration and reuse of ATP through substrate-level phosphorylation and oxidative phosphorylation, meeting the large daily energy demands of organisms.

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    ATP is the universal energy currency in biological systems. It is produced primarily through oxidative phosphorylation in the mitochondria, where a proton gradient is used by ATP synthase to catalyze the formation of ATP from ADP and inorganic phosphate. ATP is then utilized throughout the cell and hydrolyzed to drive various energy-requiring processes like biosynthesis, active transport, muscle contraction and nerve impulse transmission. The ATP-ADP cycle allows for the efficient regeneration and reuse of ATP through substrate-level phosphorylation and oxidative phosphorylation, meeting the large daily energy demands of organisms.

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    © All Rights Reserved
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    Download as pptx, pdf, or txt
    13 views27 pages

    Lecture 1 ATP

    Uploaded by

    maddie.jng
    ATP is the universal energy currency in biological systems. It is produced primarily through oxidative phosphorylation in the mitochondria, where a proton gradient is used by ATP synthase to catalyze the formation of ATP from ADP and inorganic phosphate. ATP is then utilized throughout the cell and hydrolyzed to drive various energy-requiring processes like biosynthesis, active transport, muscle contraction and nerve impulse transmission. The ATP-ADP cycle allows for the efficient regeneration and reuse of ATP through substrate-level phosphorylation and oxidative phosphorylation, meeting the large daily energy demands of organisms.

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    You are on page 1of 27

    Energy – the central role of ATP

    2B Genes, Molecules & Cells


    Professor Anna Amtmann,
    Institute of Molecular, Cell and Systems Biology

    Intro impressions: http://www.youtube.com/watch?v=nD9fyuisMkg&feature=related


    https://www.youtube.com/watch?v=XI8m6o0gXDY
    Chemical reactions require or release energy

    Exergonic: In metabolic pathways


    Amount of
    Gibbs free energy

    exergonic and
    free energy
    released
    endergonic reactions
    G<0 are often linked
    in time and space to
    minimise energy loss.
    Reactants Products

    However, in many cases


    Energy production and usage of
    energy are separated in
    Endergonic:  time and/or
    Gibbs free energy

    Amount of  space.
    free energy
    required
    G>0 We therefore need an
    ‘energy currency’.
    Reactants Products
    ATP is a ubiquitous, ancient energy currency
    Chemical structure of adenosine triphosphate
    (ATP)
    Hydrolysis of ATP

    Hydrolysis of ATP to ADP and Hydrolysis of ATP to AMP


    inorganic phosphate and pyrophosphate

    D G°’ = -7.3 kcal/mol


    (-30.5 kJ/mol) D G°’ = -10.9 kcal/mol
    (-45.6 kJ/mol)
    The ATP-ADP Cycle

    The ATP-ADP cycle is the


    fundamental mode of
    energy exchange in
    biological systems.
    Usage of ATP for biological work

    Chemical work

    Transport
    ATP

    Movement
    Usage of ATP for biological work

    Synthesis of RNA or DNA Protein synthesis

    Nucleoside monophosphate activation Amino acid activation


    Usage of ATP for biological work

    Post-translational de-/activation of proteins

    serin
    threonine
    tyrosine
    Phosphorylation sites in protein sequences
    can be predicted: e.g. NRT1.1,
    a nitrate sensor/transporter in plant roots
    1 MSLPETKSDD ILLDAWDFQG RPADRSKTGG WASAAMILCI EAVERLTTLG IGVNLVTYLT
    61 GTMHLGNATA ANTVTNFLGT SFMLCLLGGF IADTFLGRYL TIAIFAAIQA TGVSILTLST
    121 IIPGLRPPRC NPTTSSHCEQ ASGIQLTVLY LALYLTALGT GGVKASVSGF GSDQFDETEP
    181 KERSKMTYFF NRFFFCINVG SLLAVTVLVY VQDDVGRKWG YGICAFAIVL ALSVFLAGTN
    241 RYRFKKLIGS PMTQVAAVIV AAWRNRKLEL PADPSYLYDV DDIIAAEGSM KGKQKLPHTE
    301 QFRSLDKAAI RDQEAGVTSN VFNKWTLSTL TDVEEVKQIV RMLPIWATCI LFWTVHAQLT
    361 TLSVAQSETL DRSIGSFEIP PASMAVFYVG GLLLTTAVYD RVAIRLCKKL FNYPHGLRPL
    421 QRIGLGLFFG SMAMAVAALV ELKRLRTAHA HGPTVKTLPL GFYLLIPQYL IVGIGEALIY
    481 TGQLDFFLRE CPKGMKGMST GLLLSTLALG FFFSSVLVTI VEKFTGKAHP WIADDLNKGR
    541 LYNFYWLVAV LVALNFLIFL VFSKWYVYKE KRLAEVGIEL DDEPSIPMGH

    A P-site in threonine 101 provides a switch


    between high- and low-affinity nitrate uptake.
    (Ho et al. 2009 Cell 138: 1184-1194)
    Usage of ATP for biological work

    Active transport, e.g. Ca2+ pump


    Ca2+ signal in a plant guard cell.

    Ca-dependent fluorescent dye FURA2


    (Image: Mike Blatt)

    Ca2+ pumps in the plasma membrane, ER and tonoplast maintain a low cytoplasmic
    Ca2+ concentration, which is a prerequisite for fast, transient Ca2+ signals.
    Usage of ATP for biological work

    Myosin Motion Along Actin Filament


    Energy requirements & ATP turnover

    Human body:

    ATP content: 100 – 250 g (0.1 moles)

    ATP requirement/day: 50 - 75 kg!

    ATP recycled from ADP: > 500 x per day


    Regulation of energy metabolism

    High concentrations of ATP inhibit the relative rates of a typical ATP-generating


    (catabolic) pathway and stimulate the typical ATP-utilizing (anabolic) pathway.
    Sources of ATP during exercise

    Michael Johnson’s 200 m sprint


    Stored ATP: approx.1 sec
    Creatine phosphate: approx. 4 sec
    Rest: Fermentation of glucose

    Usain Bolt:
    http://www.youtube.com/watch?v=LWZQAVtkMBo
    Start 3:27
    Synthesis of ATP

    Substrate-level phosphorylation Oxidative phosphorylation


    (transfer of phosphate group) (proton gradient, ATP synthase)
    Other energy-rich phosphate bonds

    PEP
    These molecules can
    transfer their
    phosphate group to
    ADP
    BPG
    = substrate-level
    phosphorylation
    creatine phosphate

    adenosine-tri-phosphate

    ATP

    Gluc-6-P

    free energy
    Oxidative phosphorylation
    Localisation of mitochondria

    Mitochondria are often particularly numerous in ATP-consuming


    tissues and are closely associated with ATP-consuming organelles
    to maximize the speed of ATP transfer
    Structure of the ATP Synthase - general

    Rotor: spins clockwise when


    H+ ions flow past it

    Stator: holds rotor and knob in


    position

    Rod: turns with the rotor and


    activates the knob

    Knob: catalytic sites join Pi to


    ADP making ATP

    https://www.youtube.com/watch?v=PjdPTY1wHdQ
    Structure of the ATP Synthase

    10 – 14 c-subunits in the rotor

    Atomic-force micrograph Cryo-electron micrograph

    Spinach Ilyobacter
    Chloroplast tartaricus

    From: Yoshida et al. 2001 Nature Reviews


    Molecular Cell Biology 2, 669-677
    High-resolution structure by cryo-EM

    Structure of a bacterial ATP synthase eLife 2019;8:e43128 DOI:


    Hui Guo, Toshiharu Suzuki and John L. Rubinstein 10.7554/ELIFE.43128
    Cryo-EM image processing
    Solubilized protein spotted on Images of almost >1 Mio particles in
    gold-coated grid & freezing different positions

    Classification into different structures

    Model refinement

    Structure at 3 Å resolution
    Structure of the ATP Synthase - F1

    Open Loose

    Different forms of the β subunits have


    Tight different affinities for ATP and ADP

    Rotation of the γ subunit changes the conformation of the β subunits.


    Structure of the ATP Synthase - F1

    Classical model of F1 Combustion engine designed


    proposed by Paul Boyer 1977 by Felix Wankel in 1957

    From: Yoshida et al. 2001 Nature Reviews


    Molecular Cell Biology 2, 669-677
    Experimental evidence for rotation of γ
    Fluorescently labeled actin filament

    Provision of ATP drives the pump in reverse


    thus moving the γ subunit counter-clockwise.

    Noji et al. (1997) Direct observation of the rotation of F 1-ATPase Nature 386: 299–302
    The ATP synthase is reversible

    If [ATP] is low the energy of the If [ATP] is high the energy of the
    electrochemical proton gradient is phosphate bond is converted into an
    converted into chemical-bond energy electrochemical proton gradient
    (ADP + Pi -> ATP). (ATP -> ADP + Pi, proton pumping).
    ADP/ATP and Pi transport

    The ADP-ATP exchanger


    maintains low [ATP]
    in the matrix of the
    mitochondria.

    The Pi/H+ co-transporter


    imports Pi into the matrix
    Watch the movie

    ATP-production in ATP synthase: Conformational change of catalytic subunits


    https://www.youtube.com/watch?v=PjdPTY1wHdQ

    Read the textbook chapters

    Berg et al. Biochemistry Chapter 18


    Alberts et al. Molecular Biology of the Cell Chapter 14

    Dig into the science

    2014 Review: The mechanism of rotating proton pumping ATPases


    http://www.sciencedirect.com/science/article/pii/S000527281000068X

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