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    Ch 3.1. Chemical elements and water

    (taken from assessment statements)

    3. 1. 1. State that the most frequently occurring chemical elements in living things are

    carbon, hydrogen and nitrogen.

    + 3. 1. 2. State that a variety of other elements are needed by living systems, including

    sulfur, calcium, phosphorus, iron and sodium.

    + 3. 1. 3. State the role for each of the elements mentioned in 3. 1. 2.

    Symbol Name Abundance (%) (Wikipedia) Uses

    O Oxygen 65 carbohydrates, fats,

    water

    C Carbon 18 all organic compoundsH Hydrogen 10 water, all organic

    compounds

    Ca Calcium 1.5 bones, muscle

    Fe Iron H2O

    A hydrogen bond can only form when hydrogen is bonded

    to an atom with a very high electronegativity, thus

    generating a partial charge (oxygen, nitrogen and fluorine).

    3. 1. 5. Outline the thermal, cohesive and solventpro per ti es of wat er .

    + 3. 1. 6. Explain the relationship between the properties of water and its uses in living

    organisms as a coolant, medium for metabolic reactions and transport medium

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    Thermal:

    because of hydrogen bonds, a lot of energy needs to be invested to increase the kinetic energy of water

    molecules => it takes a lot of energy to change the temperature

    high thermal capacity / high specific heat (can take in a lot of energy without changing temperature greatly)

    => used in homeostasis

    high heat of vaporization (absorbs a lot of energy in vaporization) => used by perspiration

    Cohesive:

    Cohesion:molecules of the same type are attracted to one another.

    Hydrogen bonding holds molecules closer together => used in transpiration

    When solid, hydrogen bonds form a crystal structure => ice is less dense than liquid water => stays floating

    on top of lakes; turnover effect

    Adhesion: molecules of a different kind sticking to one another.

    Solvent:

    excellent solvent => reactions of polar molecules can occur in it

    hydrogen bonds can form with other molecules (ie. ethanol)

    polar solvent solves polar solute (many organic molecules, apart from fats are polar)

    The fact that water is polar and cytosol etc. is water-based affects the folding of proteins and thus the

    functionality of enzymes etc.

    Aqueous solution Location Common reactions

    cytosol from the nuclear membrane to

    the cellular membrane (apart

    from organelles)

    glycolysis, translation, many

    reactions

    nucleoplasm inside nuclear membrane transcription, DNA replicationstroma inside chloroplast (outside

    grana)

    light-independent reactions of

    photosynthesis

    matrix mitochondria cytosol Krebs cycle of respiration

    blood plasma fluid in blood transport of respiratory gases,

    nutrients and antibodies;

    clotting

    xylem fluid fluid in plant xylem water transport in plants

    sap fluid in plant phloem sugar transport in plants

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    Ch 3.2 Carbohydrates, lipids and proteins

    3. 2. 1. Distinguish between organic and inorganic compounds.

    Organic compounds are defined by the presence of carbon.

    They often include catenation of carbon. This means that carbon forms long molecules with chains of carbon

    3. 2. 2. Identify amino acids, glucose, ribose and fatty acids from diagrams showing their

    structures:

    Name Structure

    Amino acid

    Glucosesee next

    Ribose

    Fatty acid

    3. 2. 3. List three examples each of monosaccharides, disaccharides and polysaccharides

    + 3. 2. 4. State one function of glucose, lactose and glycogen in animals, and of fructose,

    sucrose and cellulose in plants.

    MonosaccharidesName Structure Use

    Ribose (D)

    / beta D ribofuranose

    present in RNA

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    Deoxyribose (beta D)

    / beta-D-ribofuranose

    present in DNA

    Glucose (D)

    / Alpha-D- glucopyranose

    blood sugar, utilized

    in glycolysis to

    obtain ATP

    Fructose (D)

    / Alpha-D-fructofuranose

    isomer of glucose,

    one of the

    monomers of

    sucrose

    Galactose (D)

    / Beta-D-galactopyranose

    monomer of lactose

    Disaccharides

    Name Structure UseLactose

    (Galactose must be beta-D, glucose can be

    beta-D or alpha-D)

    linked through beta1->4 glycosidic linkage

    Milk sugar (8-10% of milk)

    Sucrose

    alpha-D-glucopyranose and beta-D-

    fructofuranose with alpha 1->2 glycosidic

    energy source

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    linkage

    Maltose

    (Two alpha D glucopyranoses linked through

    alpha 1->4 glycosidic linkage

    Malt sugar

    Constituent of starch

    Polysaccharides

    Name Structure Use

    Amylose

    (alpha D glucopyranoses with alpha 1->4 glycosidic

    linkages)

    ~20% of starch, soluble in

    water, plant energy

    storage

    Amylopectin

    (like amylose, but additional alpha 1->6 bonds linking

    individual chains)

    ~80& of starch, insoluble

    in water, plant energy

    storage

    Glycogen

    (very similar to amylopectin, but it is impossible to tell,

    what chain is main)

    storage in animals

    Cellulose (hydrogen bonds between chains provide more stability) Cell walls, structural

    Chitin You do not need to know this! Structural, cell walls of

    fungi, exoskeletons of

    insects

    3. 2. 5. Outline the role of condensation and hydrolysis in the relationships between fatty

    acids, glycerol and triglycerides; and between amino acids and polypeptides.

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    Condensation reaction in triglycerides

    3. 2. 6. State three functions of lipids:

    1. Thermoregulation

    2.

    Energy storage

    3. Protection

    4. Membranes

    3. 2. 7. Compare the use of carbohydrates and lipids in energy storage.

    Carbohydrates Lipids better for short-term

    faster utilization (breaking up by enzymes)

    undergo glycolysis and acetyl CoA step

    same mass can result in of the energy a lipid

    could provide

    better for long-term

    slower utilization

    go straight into Krebs cycle

    same mass can result in 2x much energy as

    carbohydrate

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    Ch 3.3 DNA structure

    3. 3. 1. Outline DNA nucleotide structure in terms of sugar, base and phosphate.

    + 3. 3. 2. State the names of the four bases in DNA.

    In RNA, theres uracil:

    3. 3. 3. Outline how DNA nucleotides are linked together by covalent bonds into a single

    strand.

    + 3. 3. 4. Explain how a DNA double helix is formed using complementary base pairing and

    hydrogen bonds.

    + 3. 3. 5. Draw and label a simple

    diagram of the molecular structure of

    DNA.

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    Ch 3.4 DNA replication

    3. 4. 1. Explain DNA replication in terms of unwinding the double helix and separation of

    the strands by helicase, followed by formation of the new complementary strands by DNA

    poly me ras e.

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    3. 4. 2. Explain the significance of complementary base pairing in the conservation of the

    base sequence of DNA.

    Because base pairing is complementary, the DNA strands are also fully complementary. This means that since DNAreplication is semi-conservative, the daughter strands (newly synthesised) will be complementary to the original.

    Why? Well, if base pairing is complementary, only one base can hydrogen bond to any other base of the parent

    strand, and only the one that bonds can then be polymerized into the newly synthesised DNA strand. So, the DNA

    sequence will be conserved. (Of course, mutations can occur)

    3. 4. 3. State that DNA replication is semiconservative.

    DNA replication is semiconservative. This means, that after replication, the two DNA molecules will each contain a

    new DNA strand and an old one.

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    Ch 3.5 Transcription and translation

    3. 5. 1. Compare the structure of RNA and DNA.

    DNA RNA

    sugar 2-deoxyribose ribose

    nucleotides thymine uracil3D structure usually double helix usually single stranded

    3. 5. 2. Outline DNA transcription in terms of the formation of an RNA strand

    complementary to the DNA strand by RNA polymerase.

    This occurs in the nucleus.

    1. The sequence to be transcribed is recognized by

    TRANSCRIPTION FACTORS, which bind to it, changing

    conformation.

    2. RNA polymerase binds to the promoter

    sequencewith the help of the already bound

    transcription factor.

    3.

    RNA polymerase breaks the hydrogen bonds

    holding the two strands together.

    4.

    RNA polymerase synthesises pre-mRNA

    (direction 5->3).

    5. Upon recognition of the terminator, RNA

    synthesis is terminated.

    6.

    The RNA transcript is released and travels out of

    the nucleus through nuclear pores.

    The DNA strand read is the antisense strandand the

    mRNA sequence corresponds to that of the sense strand.

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    3. 5. 3. Describe the genetic code in terms of codons composed of triplets of bases.

    The DNA, and thus mRNA, triplets can be

    translated into amino-acids. These triplets are

    called codons.

    The genetic code is specific, but degenerate.

    Specific:one codon can only be translated to

    one amino acid only.

    Degenerate:Multiple codons can be translated

    into the same amino acid.

    It is also conservedthroughout evolution

    (there can be some exceptions , but the vast

    majority is the same).

    3. 5. 4. Explain the process of translation, leading to polypeptide formation.

    Translation involves the reading of an mRNA template and the synthesis of a polypeptide strand based on the

    genetic code.

    INITIATION

    1. Small ribosomal

    subunit scans the mRNA

    strand.

    2. First tRNA with the

    anticodon to AUG becomes

    activated with Methionine.

    (Met-tRNA-Met).

    3. Small ribosomal

    subunit (40S) recognizes

    mRNA binding site.

    4. Met-tRNA-Met

    recognizes start codon

    (AUG) on mRNA and binds

    (with hydrogen bonds.

    5.

    Large ribosomal subunit (60S) arrives and ribosome assembles.

    ELONGATION / PROPAGATION and TRANSLOCATION

    6. Met-tRNA-Met is currently at the P site of the ribosome.

    7.

    Another activated tRNA arrives at the A site (the one with the appropriate anti-codon) and binds via h-

    bonds.

    8.

    A peptide bond is formed between the Methionine and the next amino acid.

    9. Ribosome translocates along mRNA and the Met-tRNA is currently at the E site, stops bonding and leaves the

    ribosome. A new activated tRNA arrives at the A site.

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    TERMINATION

    10.

    Stop codon is not matched to any tRNA, but to the termination factor.

    11.

    Peptide is released.

    12.Ribosome disassembles.

    3. 5. 5. Discuss the relationship between one gene and one polypeptide.

    One polypeptide is coded for by one gene.

    Note that it is not true, that one protein = one gene. This is because one protein can be composed of multiple

    subunits.

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    Ch 3.6 Enzymes

    3. 6. 1. Define enzyme and active site.

    Enzymesare globular proteins acting as biological catalysts(a catalyst decreases the activation energy of a reaction

    and is not used up in the reaction).

    There are 3 main types of enzymes:

    catabolic-> catalyse the breaking up of polymers and large molecules (ie. AMYLASE -> amylose into maltose,

    LACTASE -> lactose into glucose and galactose)

    anabolic -> catalyse the synthesis of polymers and large molecules (ie. RUBISCO in photosynthesis)

    isomerases-> catalyse isomerization ( ie. from fructose to glucose)

    The active siteis an area within the 3D structure of the protein that will match the shape of the substrate and where

    reactions occur.

    3. 6. 2. Explain enzyme-substrate specificity.

    Enzymes are generally specific for substrates and reactions. This is because of the 3D shape of the enzymes active

    site, into which only the specific substrate(s) will fit.

    Lock and key model

    This model describes that an enzyme is like a lock and the substrate is the key. That is, their shapes fit completely

    and no other substrate will click no other reaction can occur. It also states that the shape of the active site is

    complementary to the shape of the substrate at all times, even when no reactions are occurring.

    This is an older and too simplified model, though.

    Induced fit model

    Unlike the lock and key model, the induced fit model does not say that the active site is perfectly fitting the substrate

    at all times. Rather, it proposes that the active site changes shape to acquire complementary to the substrate due to

    electrostatic forces etc. upon contact with the substrate. Of course, the specificity still applies.

    This model expresses reality significantly better and is presently used.

    3. 6. 3. Explain the effects of temperature, pH and substrate concentration on enzyme

    activity.

    The factor which results in lower enzyme activity (and when removed, the enzyme activity grows) is called the

    limited factor.

    Temperature

    An increase in energy means an increase in kinetic energy of the molecules.

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    pH

    (Negative logarithm of H+)

    Thus, pH is indirectly proportional to the concentration of H+

    ions (in acids, there are many H+ions and thus the pH is

    very low).

    Substrate concentration

    With growing substrate concentration, the reaction can occur

    faster (more product over same time), because the enzymes

    available will be able to catalyse the reaction of more substrates

    at the same time.

    The kinetic energy is so high

    that the enzyme is shaken so

    much, that its 3D structuregets distrupted.

    The kinetic energy makes all

    the molecules move more

    and thus it will be more likely

    for an enzyme and substrate

    to collide and meet.

    The enzyme will be more acidic than its

    environment and will therefore start

    losing hydrogens. This will break it up.

    With falling pH, there will be many

    hydrogen ions in the environment. These

    will interact with the enzyme via their

    charge (electrostatic interactions) and

    change its conformation.

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    In this graph, enzyme concentration is the limiting factor, because at a certain substrate concentration, not enough

    active sites will be available for catalysis of the reaction.

    3. 6. 4. Define denaturation.

    In denaturation, the 3D structure of an enzyme is permanently disrupted to the extent that it cannot function at all.

    3. 6. 5. Explain the use of lactase in the production of lactose-free milk.

    Lactose is a disaccharide naturally occurring in milk. Most adults on Earth (mostly of other races than Caucasian) are

    not able to digest it. Lactase is an enzyme that can digest lactose into glucose and galactose, its two constituents. If

    lactose is pre-digested by lactase prior to consumption, even lactose-intolerant people will be able to drink milk,

    because no lactose (only glucose and galactose) will be present.

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    Ch 3.7 Cell respiration

    3. 7. 1. Define cell respiration.

    Respiration is the controlled and slow series of catabolic redox reactions through which organisms extract the energy

    stored in complex molecules and use it to generate ATP (adenosine triphosphate).

    A slow and controlled oxidation of glucose occurs.

    3. 7. 2. State that, in cell respiration, glucose in the cytoplasm is broken down by glycolysis

    into pyruvate with a small yield of ATP.

    The first step of respiration is called glycolysis. This does not require oxygen and is universal in nature.

    FEEBACK INHIBITION (occurs when a high concentration of a product inhibits one of the previous steps in the

    metabolic pathway):

    glucose-6-phosphate inhibits glucoseglucose-6-phosphate

    ATP inhibits fructose-6-phosphatefructose-1,6-bisphosphate

    YIELD:

    -2ATP+4ATP = 2ATP

    2NADH+H+

    2 pyruvate

    3. 7. 3. Explain that, during anaerobic cell respiration, pyruvate can be converted in thecytoplasm with no further yield of ATP.

    Anaerobic respiration occurs when the cell lacks oxygen or the organism is anaerobic. No oxygen is needed for it.

    glucose (6C)kinase

    glucose -6-phosphate(6C) fructose -6-phosphate(6C)isomerasekinase

    fructose -1,6-bisphosphate(6C)

    ATP ADP

    ATP ADP

    dihydroxyacetone

    phosphate (3C)

    glyceraldehyde-3-phosphate (3C) 2 1,3-bisphosphoglycerate

    (3C)

    NAD+ NADH+H

    +

    2 pyruvate (3D)

    4ADP 4ATP

    PREPARATORY

    PHASE

    PAY-OFF PHASE

    2Pi

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    The first step is glycolysis, the second step is fermentation. There are 2 types of fermentation:

    ETHANOLIC FERMENTATION

    Occurs in yeast

    ( http://upload.wikimedia.org/wikipedia/commons/thumb/0/08/Ethanol_fermentation-1.svg/495px-

    Ethanol_fermentation-1.svg.png)

    LACTIC FERMENTATION

    Occurs in bacteria and animal cells deprived of

    oxygen

    (http://chsweb.lr.k12.nj.us/mstanley/outlines/respiration/image

    156.gif)

    3. 7. 4. Explain that, during aerobic cell respiration, pyruvate can be broken down in the

    mitochondrion into carbon dioxide and water with a large yield of ATP.

    In aerobic organisms, aerobic respiration can occur when there is enough oxygen in the environment. This also

    begins with glycolysis, but continues with the link reaction (acetyl-CoA step), the Krebs cycle and the electron

    transport chain.

    In the presence of oxygen, pyruvate produced in glycolysis may enter the mitochondrion, where the rest occurs.

    Note that for 1 molecule of glucose, all of the following steps must be doubled (because a pyruvate has the

    carbons of a glucose).

    LINK REACTION: (in matrix)

    Yield for 1 pyruvate:

    1 NADH+H+

    1 acetyl-CoA

    KREBS CYCLE/CITRIC ACID CYCLE: (in matrix)

    pyruvate 3C acetyl-CoA

    NAD+ NADH+H+

    CoA CO2

    http://upload.wikimedia.org/wikipedia/commons/thumb/0/08/Ethanol_fermentation-1.svg/495px-Ethanol_fermentation-1.svg.pnghttp://upload.wikimedia.org/wikipedia/commons/thumb/0/08/Ethanol_fermentation-1.svg/495px-Ethanol_fermentation-1.svg.pnghttp://upload.wikimedia.org/wikipedia/commons/thumb/0/08/Ethanol_fermentation-1.svg/495px-Ethanol_fermentation-1.svg.pnghttp://upload.wikimedia.org/wikipedia/commons/thumb/0/08/Ethanol_fermentation-1.svg/495px-Ethanol_fermentation-1.svg.pnghttp://chsweb.lr.k12.nj.us/mstanley/outlines/respiration/image156.gifhttp://chsweb.lr.k12.nj.us/mstanley/outlines/respiration/image156.gifhttp://chsweb.lr.k12.nj.us/mstanley/outlines/respiration/image156.gifhttp://chsweb.lr.k12.nj.us/mstanley/outlines/respiration/image156.gifhttp://chsweb.lr.k12.nj.us/mstanley/outlines/respiration/image156.gifhttp://chsweb.lr.k12.nj.us/mstanley/outlines/respiration/image156.gifhttp://upload.wikimedia.org/wikipedia/commons/thumb/0/08/Ethanol_fermentation-1.svg/495px-Ethanol_fermentation-1.svg.pnghttp://upload.wikimedia.org/wikipedia/commons/thumb/0/08/Ethanol_fermentation-1.svg/495px-Ethanol_fermentation-1.svg.png
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    Yield for 1 pyruvate:

    1 ATP

    1 FADH2

    3 NADH+H+

    2 CO2

    ELECTRON TRANSPORT CHAIN: (on

    cristae)

    Oxidative phosphorylationis the

    process of ATP synthesis via redox

    processes in the electron transport

    chain.

    Remember, that NADH+H+means

    that only one H is bound covalently;

    the other is floating in the cytosol.

    The electron transport chain is a

    series of membrane proteins

    including proton (H+) channels. The

    first membrane protein is

    energetically highest and each

    following is lower in energy.

    Reduced coenzymesproduced in

    previous steps have their electronand proton removed by the first

    membrane protein. As the electrons are then passed between the membrane proteins (gradually to a lower energy

    each time), the energy released can be used to pump proteinsof the coenzymes and from the cytosol across the

    citrate (6C)

    oxaloacetate (4C)

    acetyl-CoA CoA

    (5C)

    CO2

    NAD+

    NADH+H+

    several compounds (4C)

    NAD+

    NADH+H+

    CO2

    NAD+

    NADH+H+

    FADH2

    FAD+

    ATP

    ADP

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    membrane. This results in more protons in the intermembrane space and thus a negative charge of the matrix

    relative to the intermembrane space (an electrical potential, like in a battery). On the last protein (cytochrome c

    oxidase), the electrons are passed to the final electron acceptoroxygen (this is the only reason oxygen is needed

    in aerobic respiration!), along with two protons from the cytosol:

    () () () ()

    The water produced becomes a part of the matrix. The energy released in this reaction is enough to pump 1 more

    proton across the membrane.

    The electrical potential can be used as a source of energy. The membrane protein ATP synthaseis capable of

    utilizing this energy for ATP synthesis.Chemiosmosisis the movement of ions across a semipermeable membrane

    down their electrochemical gradient. Chemiosmosis of protons through the ATP synthase results in a loss of

    potential energy of these ions; this energy is used for ATP synthesis.

    FADH2has electrons with a lower energy than NADH+H+and so it enters the ETC later (at an energetically lower

    membrane protein) than the latter.

    ATP Yield from ETC:

    http://upload.wikimedia.org/wikipedia/commons/thumb/8/89/Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg/600px-Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg.png

    Note: you do not need to know other names than ATP synthase and cytochrome c oxidase (IV on picture).

    OVERALL ENERGY YIELD OF RESPIRATION

    watch this:https://www.youtube.com/watch?v=OXgOsy8yQuk

    for 1 glucose molecule

    ATP NADH+H+ FADH2

    glycolysis 2 2

    link reaction 2

    Krebs cycle 2 6 2

    total 4 10 2

    4 protons are necessary to form 1 molecule of ATP:

    1 NADH+H+10H

    +pumped2.5ATP

    1 FADH26H+pumped1.5ATP

    (Note that the result 36 is acquired when ATP yield in ETC are rounded up)

    However, remember that pyruvate is transported into the mitochondrion via active transport (ATP is used up) etc.

    http://upload.wikimedia.org/wikipedia/commons/thumb/8/89/Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg/600px-Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg.pnghttp://upload.wikimedia.org/wikipedia/commons/thumb/8/89/Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg/600px-Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg.pnghttps://www.youtube.com/watch?v=OXgOsy8yQukhttps://www.youtube.com/watch?v=OXgOsy8yQukhttps://www.youtube.com/watch?v=OXgOsy8yQukhttps://www.youtube.com/watch?v=OXgOsy8yQukhttp://upload.wikimedia.org/wikipedia/commons/thumb/8/89/Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg/600px-Mitochondrial_electron_transport_chain%E2%80%94Etc4.svg.png
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    3. 8. 6. State that ATP and hydrogen (derived from the photolysis of water) are used to fix

    carbon dioxide to make organic molecules.

    Photosynthesis can be divided into the light-dependent and light-independent reactions.

    LIGHT-DEPENDENT REACTIONS:

    products framed in pink

    The light dependent reactions are also an electron transport chain.

    LIGHT-INDEPENDENT REACTIONS (Calvin cycle):

    from primary phase framed in pink

    Photosystem II

    (P680)

    Photosystem I

    (P700)

    excitation

    of 2e-

    excitation

    of 2e-

    electron

    acce tor

    electron

    acce tor

    Plastoquinone cytochrome

    complex

    electron carriers

    pumps H

    + ATP synthase

    AT

    FerredoxinNAD

    Preductase

    NADP NADPH+H+

    PHOTOLYSIS OF WATER:

    ,()

    cyclic

    acyclic

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    3. 8. 7. Explain that the rate of photosynthesis can be measured directly by the production

    of oxygen or the uptake of carbon dioxide, or indirectly by an increase in biomass.

    The simplified equation for photosynthesis is:

    Since CO2is a reactant, its amount will decrease as the reaction proceeds.

    Since O2and C6H12O6are products of the reaction, their amount will increase as the reaction proceeds.

    3. 8. 8. Outline the effects of temperature, light intensity and carbon dioxide concentration

    on the rate of photosynthesis.

    (See enzymes)

    Carbon dioxide is a substrate.

    Light intensity:

    6 CO2 (1C)

    6 (6C) unstable

    intermediate

    12 glycerate-3-

    phosphate (3C)

    6 ribulose

    bisphosphate

    (RuBP) (5C)

    12 triose

    phosphate (3C)

    10 triose

    phosphate (3C)

    6ADP

    6ATP

    4Pi

    12ATP

    12ADP

    12NADPH+H+

    12NADP+

    2 triose

    phosphate (3C)

    sugar phosphates

    (6C)Pi complex carbohydrates

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    . (http://www2.geog.ucl.ac.uk/~plewis/geogg124/_images/chapin1.png)