How Does Atp Synthase Obtain the Energy to Produce Atp

How Does Atp Synthase Obtain the Energy to Produce Atp.

Enzyme

ATP Synthase
Atp synthase.PNG

Molecular model of ATP synthase adamant by X-ray crystallography. Stator is non shown here.

Identifiers
EC no. seven.1.two.2
CAS no. 9000-83-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

ATP synthase
is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi). It is classified under ligases as it changes ADP by the formation of P-O bond (phosphodiester bond). ATP synthase is a molecular automobile. The overall reaction catalyzed by ATP synthase is:

  • ADP + Pi
    + 2H+
    out
    ⇌ ATP + H2O + 2H+
    in

The formation of ATP from ADP and Pi
is energetically unfavorable and would normally proceed in the contrary direction. In order to drive this reaction frontwards, ATP synthase couples ATP synthesis during cellular respiration to an electrochemical gradient created by the divergence in proton (H+) concentration across the inner mitochondrial membrane in eukaryotes or the plasma membrane in leaner. During photosynthesis in plants, ATP is synthesized by ATP synthase using a proton gradient created in the thylakoid lumen through the thylakoid membrane and into the chloroplast stroma.

Eukaryotic ATP synthases are F-ATPases, running “in reverse” for an ATPase. This article deals mainly with this type. An F-ATPase consists of two main subunits, FO
and F1, which has a rotational motor mechanism allowing for ATP production.[i]
[two]

Nomenclature

[edit]

The Fane
fraction derives its proper name from the term “Fraction 1” and FO
(written as a subscript letter “o”, not “cipher”) derives its name from existence the binding fraction for oligomycin, a blazon of naturally derived antibody that is able to inhibit the FO
unit of ATP synthase.[3]
[4]
These functional regions consist of different protein subunits — refer to tables. This enzyme is used in synthesis of ATP through aerobic respiration.

Structure and function

[edit]

Bovine mitochondrial ATP synthase. The FO, Fane, axle, and stator regions are color coded magenta, light-green, orange, and cyan respectively.[v]
[6]

Simplified model of FOF1-ATPase alias ATP synthase of
E. coli. Subunits of the enzyme are labeled appropriately.

Rotation engine of ATP synthase.

Located inside the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of 2 regions FO
and Fone. FO
causes rotation of Fi
and is fabricated of c-ring and subunits a, two b, F6. F1
is fabricated of α, β, γ, and δ subunits. F1
has a water-soluble part that can hydrolyze ATP. FO
on the other hand has mainly hydrophobic regions. FO
Fone
creates a pathway for protons move beyond the membrane.[7]

F1
region


[edit]

The F1
portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. The Fane
unit of measurement protrudes into the mitochondrial matrix space. Subunits α and β make a hexamer with 6 binding sites. Three of them are catalytically inactive and they demark ADP.

Iii other subunits catalyze the ATP synthesis. The other Fane
subunits γ, δ, and ε are a part of a rotational motor mechanism (rotor/axle). The γ subunit allows β to go through conformational changes (i.e., closed, half open, and open up states) that allow for ATP to be bound and released in one case synthesized. The Fane
particle is large and tin can exist seen in the transmission electron microscope by negative staining.[eight]
These are particles of ix nm diameter that pepper the inner mitochondrial membrane.

F1
– Subunits[9]
Subunit Human Cistron Note
alpha ATP5A1, ATPAF2
beta ATP5B, ATPAF1
gamma ATP5C1
delta ATP5D Mitochondrial “delta” is bacterial/chloroplastic epsilon.
epsilon ATP5E Unique to mitochondria.
OSCP ATP5O Called “delta” in bacterial and chloroplastic versions.

FO
region


[edit]

FO
subunit F6 from the peripheral stalk region of ATP synthase.[10]

FO
is a water insoluble protein with eight subunits and a transmembrane ring. The ring has a tetramer shape with a helix loop helix protein that goes through conformational changes when protonated and deprotonated, pushing neighboring subunits to rotate, causing the spinning of FO
which and so also affects conformation of F1, resulting in switching of states of alpha and beta subunits. The FO
region of ATP synthase is a proton pore that is embedded in the mitochondrial membrane. Information technology consists of 3 master subunits, a, b, and c. Six c subunits brand upwardly the rotor ring, and subunit b makes up a stem connecting to Fane
OSCP that prevents the αβ hexamer from rotating. Subunit a connects b to the c band.[11]
Humans accept six additional subunits, d, e, f, thousand, F6, and 8 (or A6L). This part of the enzyme is located in the mitochondrial inner membrane and couples proton translocation to the rotation that causes ATP synthesis in the F1
region.

In eukaryotes, mitochondrial FO
forms membrane-angle dimers. These dimers self-suit into long rows at the terminate of the cristae, possibly the first step of cristae formation.[12]
An diminutive model for the dimeric yeast FO
region was determined by cryo-EM at an overall resolution of 3.half-dozen Å.[xiii]

FO-Main subunits
Subunit Human Gene
a MT-ATP6
b ATP5F1
c ATP5G1, ATP5G2, ATP5G3

Binding model

[edit]

Mechanism of ATP synthase. ADP and Pi
(pink) shown being combined into ATP (red), while the rotating γ (gamma) subunit in blackness causes conformational change.

In the 1960s through the 1970s, Paul Boyer, a UCLA Professor, adult the bounden change, or flip-flop, mechanism theory, which postulated that ATP synthesis is dependent on a conformational change in ATP synthase generated by rotation of the gamma subunit. The inquiry group of John Due east. Walker, then at the MRC Laboratory of Molecular Biological science in Cambridge, crystallized the Fone
catalytic-domain of ATP synthase. The construction, at the fourth dimension the largest asymmetric protein structure known, indicated that Boyer’s rotary-catalysis model was, in essence, correct. For elucidating this, Boyer and Walker shared one-half of the 1997 Nobel Prize in Chemistry.

The crystal structure of the F1
showed alternate alpha and beta subunits (3 of each), bundled like segments of an orangish around a rotating asymmetrical gamma subunit. According to the current model of ATP synthesis (known equally the alternating catalytic model), the transmembrane potential created by (H+) proton cations supplied by the electron ship chain, drives the (H+) proton cations from the intermembrane infinite through the membrane via the FO
region of ATP synthase. A portion of the FO
(the band of c-subunits) rotates as the protons laissez passer through the membrane. The c-band is tightly attached to the asymmetric primal stalk (consisting primarily of the gamma subunit), causing information technology to rotate within the blastoff3beta3
of Fane
causing the 3 catalytic nucleotide binding sites to go through a serial of conformational changes that lead to ATP synthesis. The major F1
subunits are prevented from rotating in sympathy with the fundamental stalk rotor by a peripheral stalk that joins the alphaiiibeta3
to the non-rotating portion of FO. The construction of the intact ATP synthase is currently known at depression-resolution from electron cryo-microscopy (cryo-EM) studies of the circuitous. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps effectually the circuitous as it joins F1
to FO. Under the right conditions, the enzyme reaction can also be carried out in contrary, with ATP hydrolysis driving proton pumping across the membrane.

The binding change mechanism involves the active site of a β subunit’s cycling betwixt three states.[14]
In the “loose” state, ADP and phosphate enter the active site; in the adjacent diagram, this is shown in pink. The enzyme and then undergoes a change in shape and forces these molecules together, with the active site in the resulting “tight” state (shown in red) binding the newly produced ATP molecule with very high analogousness. Finally, the active site cycles back to the open state (orangish), releasing ATP and binding more ADP and phosphate, ready for the side by side bike of ATP product.[15]

Physiological office

[edit]

Like other enzymes, the action of FaneFO
ATP synthase is reversible. Large-enough quantities of ATP cause it to create a transmembrane proton gradient, this is used by fermenting bacteria that do not take an electron transport chain, only rather hydrolyze ATP to make a proton gradient, which they use to drive flagella and the transport of nutrients into the jail cell.

In respiring bacteria under physiological conditions, ATP synthase, in full general, runs in the contrary direction, creating ATP while using the proton motive force created by the electron transport chain as a source of free energy. The overall process of creating free energy in this fashion is termed oxidative phosphorylation. The same process takes place in the mitochondria, where ATP synthase is located in the inner mitochondrial membrane and the F1-part projects into the mitochondrial matrix. By pumping proton cations into the matrix, the ATP-synthase converts ADP into ATP.

Evolution

[edit]

The evolution of ATP synthase is thought to have been modular whereby two functionally independent subunits became associated and gained new functionality.[xvi]
[17]
This clan appears to have occurred early on in evolutionary history, because substantially the same structure and activity of ATP synthase enzymes are present in all kingdoms of life.[16]
The F-ATP synthase displays high functional and mechanistic similarity to the V-ATPase.[18]
However, whereas the F-ATP synthase generates ATP past utilising a proton slope, the Five-ATPase generates a proton gradient at the expense of ATP, generating pH values of as low as 1.[19]

The F1
region as well shows pregnant similarity to hexameric Deoxyribonucleic acid helicases (especially the Rho factor), and the unabridged enzyme region shows some similarity to
H
+



-powered T3SS or flagellar motor complexes.[xviii]
[20]
[21]
The αiiiβ3
hexamer of the F1
region shows significant structural similarity to hexameric Dna helicases; both course a ring with 3-fold rotational symmetry with a primal pore. Both have roles dependent on the relative rotation of a macromolecule inside the pore; the DNA helicases apply the helical shape of DNA to drive their motion along the DNA molecule and to notice supercoiling, whereas the αthreeβ3
hexamer uses the conformational changes through the rotation of the γ subunit to bulldoze an enzymatic reaction.[22]

The
H
+




motor of the FO
particle shows cracking functional similarity to the
H
+




motors that bulldoze flagella.[18]
Both feature a ring of many pocket-sized alpha-helical proteins that rotate relative to nearby stationary proteins, using a
H
+




potential gradient as an free energy source. This link is tenuous, still, as the overall structure of flagellar motors is far more complex than that of the FO
particle and the ring with about xxx rotating proteins is far larger than the x, 11, or 14 helical proteins in the FO
complex. More recent structural information do however testify that the ring and the stalk are structurally similar to the F1
particle.[21]

Conformation changes of ATP synthase during synthesis

The modular evolution theory for the origin of ATP synthase suggests that two subunits with contained function, a Dna helicase with ATPase activity and a
H
+




motor, were able to bind, and the rotation of the motor drove the ATPase activeness of the helicase in reverse.[16]
[22]
This complex and so evolved greater efficiency and somewhen developed into today’s intricate ATP synthases. Alternatively, the DNA helicase/H
+




motor complex may accept had
H
+




pump action with the ATPase activity of the helicase driving the
H
+




motor in opposite.[16]
This may take evolved to behave out the reverse reaction and human activity as an ATP synthase.[17]
[23]
[24]

Inhibitors

[edit]

A variety of natural and synthetic inhibitors of ATP synthase have been discovered.[25]
These have been used to probe the structure and mechanism of ATP synthase. Some may exist of therapeutic apply. At that place are several classes of ATP synthase inhibitors, including peptide inhibitors, polyphenolic phytochemicals, polyketides, organotin compounds, polyenic α-pyrone derivatives, cationic inhibitors, substrate analogs, amino acid modifiers, and other miscellaneous chemicals.[25]
Some of the most commonly used ATP synthase inhibitors are oligomycin and DCCD.

In unlike organisms

[edit]

Bacteria

[edit]




Eastward. coli


ATP synthase is the simplest known course of ATP synthase, with 8 different subunit types.[xi]

Bacterial F-ATPases can occasionally operate in reverse, turning them into an ATPase.[26]
Some leaner have no F-ATPase, using an A/V-type ATPase bidirectionally.[ix]

Yeast

[edit]

Yeast ATP synthase is i of the best-studied eukaryotic ATP synthases; and five Fone, eight FO
subunits, and seven associated proteins take been identified.[7]
Near of these proteins take homologues in other eukaryotes.[27]
[28]
[29]
[30]

Plant

[edit]

In plants, ATP synthase is also nowadays in chloroplasts (CFaneFO-ATP synthase). The enzyme is integrated into thylakoid membrane; the CFane-part sticks into stroma, where dark reactions of photosynthesis (too chosen the light-independent reactions or the Calvin wheel) and ATP synthesis have place. The overall structure and the catalytic machinery of the chloroplast ATP synthase are well-nigh the same as those of the bacterial enzyme. However, in chloroplasts, the proton motive force is generated not by respiratory electron transport chain but by primary photosynthetic proteins. The synthase has a 40-aa insert in the gamma-subunit to inhibit wasteful action when dark.[31]

Mammal

[edit]

The ATP synthase isolated from bovine (Bos taurus) eye mitochondria is, in terms of biochemistry and structure, the all-time-characterized ATP synthase. Beefiness eye is used equally a source for the enzyme considering of the high concentration of mitochondria in cardiac muscle. Their genes have close homology to human being ATP synthases.[32]
[33]
[34]

Homo genes that encode components of ATP synthases:

  • ATP5A1
  • ATP5B
  • ATP5C1, ATP5D, ATP5E, ATP5F1, ATP5G1, ATP5G2, ATP5G3, ATP5H, ATP5I, ATP5J, ATP5J2, ATP5L, ATP5O
  • MT-ATP6, MT-ATP8

Other eukaryotes

[edit]

Eukaryotes belonging to some divergent lineages have very special organizations of the ATP synthase. A euglenozoa ATP synthase forms a dimer with a boomerang-shaped Fi
head like other mitochondrial ATP synthases, merely the FO
subcomplex has many unique subunits. It uses cardiolipin. The inhibitory IFone
likewise binds differently, in a way shared with trypanosomatida.[35]

Archaea

[edit]

Archaea do not generally have an F-ATPase. Instead, they synthesize ATP using the A-ATPase/synthase, a rotary machine structurally similar to the V-ATPase just mainly functioning as an ATP synthase.[26]
Similar the bacteria F-ATPase, information technology is believed to also function as an ATPase.[9]

LUCA and earlier

[edit]

F-ATPase gene linkage and factor lodge are widely conserved across ancient prokaryote lineages, implying that this organization already existed at a appointment before the last universal mutual ancestor, the LUCA.[36]

See also

[edit]

  • ATP10 protein required for the associates of the FO
    sector of the mitochondrial ATPase complex.
  • Chloroplast
  • Electron transfer chain
  • Flavoprotein
  • Mitochondrion
  • Oxidative phosphorylation
  • P-ATPase
  • Proton pump
  • Rotating locomotion in living systems
  • Transmembrane ATPase
  • V-ATPase

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[edit]


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Further reading

[edit]

  • Nick Lane:
    The Vital Question: Free energy, Evolution, and the Origins of Complex Life, Ww Norton, 2015-07-20, ISBN 978-0393088816 (Link points to Effigy 10 showing model of ATP synthase)

External links

[edit]

  • Boris A. Feniouk: “ATP synthase — a splendid molecular machine”
  • Well illustrated ATP synthase lecture by Antony Crofts of the University of Illinois at Urbana–Champaign.
  • Proton and Sodium translocating F-type, 5-type and A-blazon ATPases in OPM database
  • The Nobel Prize in Chemical science 1997 to Paul D. Boyer and John E. Walker for the enzymatic mechanism of synthesis of ATP; and to Jens C. Skou, for discovery of an ion-transporting enzyme,
    Na
    +



    ,
    K
    +



    -ATPase.
  • Harvard Multimedia Product Site — Videos – ATP synthesis animation
  • David Goodsell: “ATP Synthase- Molecule of the Month”



How Does Atp Synthase Obtain the Energy to Produce Atp

Source: https://en.wikipedia.org/wiki/ATP_synthase