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APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

SLIDE 00: Photosynthesis


Photosynthesis begins with the light-dependent
reactions which occurs in the thylakoid membranes of
the chloroplast. These reactions purpose is to harness
light energy and convert it into usable chemical energy.
Light is initially absorbed via P680 of photosystem II,
exciting the chlorophyll molecule and bringing the
molecules electron at a higher energy state. The
released electron will then be replaced by an electron
produced via photolysis or the splitting of H2O into H+
and O2. Meanwhile, energy from the released electron
is harvested by an electron transport system (ETS) until
the electron reaches P700 in photosystem I. When the
electron in P700 is then excited by another photon,
energy will again be harvested by another ETS. The
electrons endpoint in the second ETS is the conversion
of NADP+ to NADPH.
The harvested energy from PSI and PSII is in
the form of ATP. ATP may also be harvested via the
cyclic electron flow or cyclic photophosphorylation.
Energy from an excited electron from P700 of PSI is
gathered by an electron transport system ending in
plastocyanin which carries back the electron to P700.
The ATP and NADPH produced in the light
reactions are utilized in the Calvin-Benson Cycle or the
light-independent reactions. In this process, organic
molecules are formed from atmospheric CO2. The key
step in the Calvin cycle is the binding of CO2 to ribulose
1,5-bisphosphate (RuBP). The enzyme that carries out
this
reaction
is
ribulose
bisphosphate
carboxylase/oxygenase (usually abbreviated rubisco)
(McGraw Hill, 2007). The five-carbon RuBP, together
with a four-carbon sugar, is formed from the binding of
fructose 6-phosphate and glyceraldehyde 3-phosphate.

BIO 150 LEC 2

SLIDE 2:
It would be safe to assume that not all colors of
lights (wavelengths) have the same energy levels. And
based on the equation above, energy can be said to be
inversely proportional to wavelength. Einsteins theory
of the photoelectric effect provides an explanation:
sunlight contains photons of many different energy
levels, only some of which our eyes perceive as visible
light. As photons are the fundamental particles of light,
they are only expected that its state can reflect what
type, wavelength, and color of light they possess
(Buchanan et al., 2015).
Before any kind of light energy can be utilized
by any system, it is firstly absorbed. For photosynthetic
organisms, this is important, as light energy is its
primary source. So any actions that could shade or
reflect the light that should have been absorbed by the
plant is detrimental, as it can possibly result in large
losses of available light (Buchanan et al., 2015). In
plants, algae, and cyanobacteria, pigments are the means
by which the energy of sunlight is captured for
photosynthesis. However, since each pigment reacts
with only a narrow range of the spectrum, there is
usually a need to produce several kinds of pigments,
each of a different color, to capture more the suns
energy. There are three basic classes of pigments:
chlorophylls, carotenoids, and phycobilins. Among
them, chlorophylls serve to be the most common of the
group (University of California Museum of
Paleontology, 1997).
The most important chlorophyll is said to be
chlorophyll a, as this molecule makes photosynthesis
possible (passes its energized electrons on to molecules
which will manufacture sugars). Other chlorophylls
include chlorophyll b and chlorophyll c. Chlorophyll a
& b are green and are able to best absorb light in the
450 nm (violet-blue) and 650 nm (red) area of the light
spectrum. Well, that leaves the green, yellow and
orange parts of the spectrum unusable. This is why
plants have extra pigments (colors), in order to take in
light from different wavelengths that chlorophyll is not
good at absorbing (University of California Santa
Barbara, 2015).

APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

SLIDE 3: Spectrophotometer technique


An instrument called the spectrophotometer
measures the ability of a pigment to absorb various
wavelengths of light. This machine sends beams of light
of different wavelengths through a solution of the
pigment and measures the fraction of light transmitted at
each wavelength.
In the figure, passing white light through a
prism separates the light into different wavelengths,
appearing as a rainbow of colors. The order of the
colors is determined by the wavelength of light. For
visible light, red has the longest wavelength while violet
has the shortest wavelength. However, visible light is
just a small portion of the electromagnetic spectrum
where energy is inversely proportional to the
wavelength.
A pigment is any substance that absorbs light.
The color of the pigment comes from the wavelengths
of light that are reflected, or in other words, those
wavelengths not absorbed. One by one, the different
colors of light are passed through the sample
chlorophyll solution. Green light and blue light are
shown in the figure.
This transmitted light strikes a material that
converts the light energy to electricity called a
photoelectric tube. The electric current generated is
measured by a galvanometer. This meter indicates the
fraction of light transmitted through the sample where
we can determine the amount of light absorbed. The
galvanometer shows that chlorophyll absorbs very little
green light (high transmittance) which is why plants
appear green to us. On the other hand, chlorophyll
absorbs most blue light (low transmittance) which
works best for photosynthesis.

BIO 150 LEC 2

Slide 4: Chlorophylls are the key pigment molecules


driving photosynthesis. Chlorophyll a is the main
photosynthetic pigment. All photosynthetic plants, algae
and cyanobacteria contain chlorophyll a. Accessory
pigments like chlorophyll b and carotenoids broaden the
spectrum. Chlorophyll b occurs only in plants and in
green algae. Carotenoids are usually red, orange, or
yellow pigments, and include the familiar compound
carotene. They absorb excess light that may damage the
chlorophylls. However, they cannot transfer energy
from sunlight directly to the photosynthetic pathway,
but must pass their absorbed energy to chlorophyll. For
this reason, they are called accessory pigments (Speer,
1995).
An absorption spectrum is a graph plot of a
pigments light absorption versus wavelength. Violetblue and red light work best for photosynthesis. Green
and yellow lights are absorbed very little (Speer, 1995).
An action spectrum profiles the relative
effectiveness of different wavelengths of radiation in
driving a process. It ratifies the pigments actually
involved in the photosynthesis (Speer, 1995). Examples
of effects measured by action spectra are oxygen
evolution and hormonal growth responses due to the
action of phytochrome. Action spectra were
instrumental in the discovery of the existence of the two
photosystems in Oxygen-evolving photosynthetic
organisms. T.W. Engelmann, in the late 1800s, used a
prism to disperse sunlight into a rainbow that was
allowed to fall on an aquatic algal filament. A
population of O2-seeking bacteria was introduced into
the system. The bacteria congregated in the regions of
the filaments that evolved the most O2. These were the
regions illuminated by blue light and red light, which
are strongly absorbed by chlorophyll (Taiz et al., 2015).

APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

BIO 150 LEC 2


therefore be used for the light reactions (Raven et al,
2005).

SLIDE 5: Chlorophyll Molecule Excitation


Chlorophyll molecules in their excited state
may decay into its original energy state in three possible
ways a) energy may be converted exclusively to heat
energy via movement of molecules, or a combination of
heat and light of long wave length as used in
fluorescence; b) extra energy, not the electron, may be
transferred to a neighboring chlorophyll molecule via
resonance energy transfer and is used for increasing the
energy level of an electron in this adjacent molecule
and; c) the excited chlorophyll molecule may become an
electron donor and transfers the high energy electron to
a nearby molecule.

SLIDE 6: In 1982, two plant physiologists, Robert


Emerson and William Arnold, performed an experiment
on an organism that enabled them to approximately
scale the dependence of the output of photosynthesis on
the intensity of illumination, like how much
photosynthesis occurs by how much light. This was
achieved by measuring the number of chlorophyll
molecules and the output of the photosynthesis of the
subjects (Chlorella). There is however, the concept of
saturation. This is when the light-absorbing capacity of
the plant is reached, and thus even if there is available
light, this will not increase the final output. In their
experiment, therefore, they expected results that would
mirror this concepts principle. This would mean when
there is stronger light, the yield will increase, until every
chlorophyll molecule reaches its most excited state, and

However, the result was different. The


saturation point was achieved much quicker. This led to
the pair to conclude that absorption of light was not
done independently, but instead by clusters. These
clusters of chlorophylls are associated with accessory
pigments that kind of assist them. Along with numerous
associated proteins held within a protein matrix on the
surface of the chloroplast membrane, the pigment
molecules and accessory pigments forms a photosystem
(Raven et al, 2005).
Photosystems, in order to achieve this, requires
two closely linked components. In the first, light is
absorbed by antennae, proteins that bind several
chlorophyll molecules. In many cases, a large number of
antennae proteins are available to trap light energy.
Chlorophylls that absorb light can pass on this energy to
other adjacent pigments in a process called exciton
transfer. The structure and organization of antennae
protein systems reveals that these proteins function as
scaffolds that ligate their chlorophylls in highly
organized complexes. In many cases, the excitons
generated in antennae are transferred to the second
category of photoactive protein complexes that are
known as reaction centers. These reaction centers are
multisubunit membrane protein complexes that function
as remarkable photochemical devices. They capture
energy by either exciton transfer from antennae, or by
direct absorption of light by chlorophyll. This light
energy is then converted into oxidation-reduction
potential energy, and is stabilized in the reaction center
in a form that has a lifetime sufficiently long
(milliseconds) to permit electrons to be extracted from
the system. The transfer of these electrons to other
redox enzymes is used to generate the ion and pH
gradients that provide the energy for ATP synthesis, as
well as the reducing power that is used for conversion of
CO2 into sugars, starch and other metabolites (Russell
et al., 2014)
To be more specific, reaction centers enable
the conversion of light energy to chemical energy. This
occurs when there exists energy transfer around the
reaction centers. For example, when a reaction center
gives off a light-energized electron to the primary
electron acceptor, a reduction occurs (converts the
acceptor to a strong electron donor). This is only
possible if the reaction center chlorophyll, itself, was
energized, therefore creating a strong electron donor.
The oxidized chlorophyll then fills its electron
deficiency by oxidizing a weak donor molecule, thereby

APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

BIO 150 LEC 2

restoring the chlorophyll to its original condition. In


plant chloroplasts, water serves as the electron donor
(Raven et al, 2005).

Slide 8: The Reaction Center of Purple Bacteria

SLIDE 7: Antenna complex and photochemical reaction


center in a photosystem
Multiprotein complexes called photosystems
catalyze the conversion of the light energy captured in
excited chlorophyll molecules to useful forms. A
photosystem consists of two closely linked components
namely the antenna complex which consists of large set
of pigment molecules that capture the light energy and
feed it to the reaction center; and the photochemical
reaction center which consists complex of proteins and
chlorophyll molecules that enable light energy to be
converted into chemical energy.
The antenna complex is important in capturing
light. It is a collector of light energy in the form of
excited electrons. It consists of a number of distinct
protein
light-harvesting
complexes
from
the
chloroplasts that binds with several hundred
chlorophylls per reaction center orienting them precisely
in the thylakoid membrane. When a chlorophyll
molecule in the antenna complex is excited, the energy
is rapidly transferred from one molecule to another by a
series of resonance transfers until it reaches a special
pair of chlorophyll molecules in the photochemical
reaction center. Each antenna complex collects light
energy and directs it to a specific site where it can be
used effectively hence, acts as a funnel.
The photochemical reaction center is a
transmembrane protein pigment complex that lies at the
heart of photosynthesis. The special pair of chlorophyll
molecules in the reaction center acts as an irreversible
trap for excitation quanta because the excited electron is
passed rapidly to the electron transport chain in the
thylakoid membrane via a quinone.

The structure is comprised of three proteins


called L, M, and H (Low, Medium, High) after their
apparent molecular masses on an SDS PAGE. The L-MH terminology is still in use, but DNA sequencing has
resulted in a revision of the molecular masses, so that LM-H is no longer accurate. The H subunit on the side of
the reaction center accepts the electrons released by the
absorption of photons, and the cytochrome subunit
ligates the electron donor hemes (Ort & Yocum, 1996).
The Reaction Center of Photosystem II
The structure of PSII is remarkably similar to
the bacterial reaction center and it is theorized that they
share a common ancestor. The core of PSII consists of
two subunits referred to as D1 and D2, which are
similar to the L and M subunits present in the bacterial
reaction center. PSII differs from the bacterial reaction
centers in that it has many additional subunits which
bind additional chlorophylls to increase efficiency
(McGill, 2007).
The Reaction Center of Photosystem I
The final stage of the light reactions is
catalyzed by PSI. PSI has two main components
forming its core, psaA and psaB. These two subunits are
quite larger than the core components of PSII and the
bacterial photosystem. Nonetheless, the subunits are all
homologous. The electron donor would be the reduced
plastocyanin (Miles, 2003).

APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

BIO 150 LEC 2


bound protein analogous to Complex III of the
mitochondrial electron transport chain) to Photosystem I
(Raven et al., 2005).

SLIDE 10: Thylakoid Membrane Electron Transport


System
When a photon enters PSI, it excites an
electron which is then coupled with a proton produced
from the splitting of water. The oxygen also produced
from photolysis becomes a by-product and exits the cell
whereas the hydrogen ions remain in the thylakoid
space. The electron will then be passed along a series of
cytochrome electron carriers. At cytochrome b6-f
complex, energy carried by the electron is utilized for
the pumping of a hydrogen ion into the thylakoid space.
Thus, H+ concentration becomes higher within the
thylakoid. When another photon strikes the thylakoid at
PSI, a second electron is excited and passed through a
reduction complex, which generates NADPH (McGraw
Hill, 2007).

Photosystem II (PS II) is the first link in the


chain of photosynthesis. It captures photons and uses
the energy to extract electrons from water molecules.
The 4 electrons removed from the water molecules are
transferred by an electron transport chain to ultimately
reduce 2NADP+ to 2NADPH. During the electron
transport process a proton gradient is generated across
the thylakoid membrane. This proton motive force is
then used to drive the synthesis of ATP (Raven et al.,
2005). This occurs when electrons are transferred from
water to plastoquinone.
Plastoquinone (PQ) carries the electrons from
PSII to the cytochrome bf complex. Plastoquinone is an
analog of Coenzyme Q. The only differences are the
methyl groups replacing the methoxy groups of Q and a
variable isoprenoid tail. Plastoquinone can functions as
a one or two electron acceptor and donor. When it is
fully reduced to PQH2 it is called plastoquinol. Like
CoQ, PQ is a lipophilic mobile electron carrier carrying
electrons from PSII to cytochrome bf.
The overall reaction of PSII is shown below.
2PQ + 2H2O -> O2 +2PQH2

SLIDE 11:
Two photosystems exist within the thylakoid
membranes of the chloroplast. These photosystems use
a collection of highly-colored molecules to capture
light. These light-absorbing molecules include green
chlorophylls, which are composed of a flat organic
molecule surrounding a magnesium ion, and orange
carotenoids, which have a long string of carbon-carbon
double bonds. These molecules absorb light and use it to
energize electrons. The high-energy electrons are then
harnessed to power the cell. Photosystem I optimally
absorbs light wavelengths of 700 nm. Photosystem II
optimally absorbs photons of a wavelength of 680 nm.
The numbers indicate the order in which the
photosystems were discovered, not the order of electron
transfer. Under normal conditions electrons flow from
Photosystem II through cytochrome bf (a membrane

The plastoquinol formed by PSII contributes its


electrons through an electron transport chain that
terminates at PSI. The intermediary electron transfer
complex between PSII and PSI is cytochrome bf also
known as cytochrome b6f. In this electron transfer
complex electrons are passed one at a time from
plastoquinol to plastocyanin (Pc) a copper protein of the
thylakoid lumen. The protons are released into the
thylakoid lumen.
The reaction is shown below:
PQH2 +2Pc(Cu2+) -> 2Pc(Cu+) + 2H+
Plastocyanin is a water soluble electron carrier
found in the thylakoid lumen of chloroplasts. It contains
a single Copper atom coordinated to two histidine
residues and a cysteine residue in a distorted
tetrahedron. The molecule is intensely blue in the cupric
form. This mobile electron carrier carries electrons from
cytochrome bf to PSI.
The cytochrome bf contains two b-type heme
cytochromes, a Reiske protein-type Fe-S protein, and a
c type cytochrome similar to cytochrome c1. This
enzyme transfers electrons from plastoquinol through

APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

BIO 150 LEC 2

the same Q cycle as Complex III. The net result is two


protons are picked up from the stroma side of the
thylakoid membrane and 4 protons are released into the
lumen contributing to the pH gradient.
The final stage of the light reactions is
catalyzed by PSI. A special pair of chlorophyll a
molecules lies at the center of the structure which
absorbs light maximally at 700 nm. This special pair is
denoted P700. Upon excitation-either by direct
absorption of a photon or exciton transfer- P700*
transfers an electron through a chlorophyll and a bound
quinone (QA) to a set of 4Fe-4S clusters. From these
clusters the electron is transferred to ferredoxin (Fd) a
water soluble mobile electron carrier located in the
stroma which contains a 2Fe-2S cluster coordinated to 4
cysteine residues. The electron transfer produces a
positive charge on the special pair which is neutralized
by the transfer of an electron from a reduced
plastocyanin.
The overall reaction is shown below.
Pc(Cu+) + Fdox -> Pc(Cu2+) + Fdred
The electron acceptor in the overall reaction is
the oxidized ferredoxin, the electron donor is the
reduced plastocyanin. This uphill electron transfer is
driven the by absorption of a 700-nm photon of light.
Ferredoxin is a strong reductant but can only function in
one electron reductions. NADP+ can only accept 2
electrons in the form of a hydride. The transfer of
electrons from reduced ferredoxin to NADP+ it
catalyzed by ferredoxin-NADP+ reductase which is
flavoprotein. This complex contains a tightly bound
FAD which accepts the electrons one at a time from
ferredoxin. The FADH2 then transfers a hydride to
NADP+ to form NADPH (Raven et al., 2005).
Photosystem I (PS I)
PS I is located at the outer
surface of the grana
thylakoid membrane.
The photocenter is P700.
Pigments absorb longer
wavelengths
of
light
(>680nm).
Participates in cyclic as
well
as
non-cyclic
photophosphorylation.
It is not associated with
photolysis of water.
Main function is ATP
synthesis.

Photosystem II (PS II)


PS II is located at the inner
surface of the grana
thylakoid membrane
The photocenter is P680.
Pigments absorb shorter
wavelengths
of
light
(<680nm).
Participates only in noncyclic
photophosphorylation.
It is associated with
photolysis of water.
Main functions are ATP
synthesis and hydrolysis
of water.

SLIDE 12: Changes in redox potential during


photosynthesis
The redox potential for each molecule is
indicated by its position along the vertical axis. This
scheme for photosynthesis is known as the Z scheme
with two electron-energizing steps: one catalyzed by
each photosystem where an electron is passed from
water which normally holds on to its electrons very
tightly (redox potential = +820 mV), to NADPH that
holds on to its electrons loosely (redox potential = -320
mV). In photosystem II, the excited reaction center
chlorophyll has a redox potential high enough to
withdraw electrons from water by organized cluster of
four manganese atoms. Photosystem II then passes
electrons from its excited chlorophyll to an electrontransport chain that leads to photosystem I. However,
there is not enough energy in a single quantum of
visible light to energize an electron all the way from the
bottom of photosystem II to the top of photosystem I,
which is presumably the energy change required to pass
an electron efficiently from water to NADP+. The use
of two separate photosystems in series means that the
energy from two quanta of light is available for this
purpose. Photosystem I then passes electrons from its
excited chlorophyll through a series of tightly bound
iron-sulfur centers. This net electron flow through the
two photosystems in series is from water to NADP+,
and it produces NADPH as well as ATP.

Slide 13: In special cases, photoexcited electrons


photoexcited electrons can follow an alternative path

APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

BIO 150 LEC 2

called cyclic electron flow, which uses photosystem I


but not photosystem II (Sadava et al., 2009).
Characterized as a short circuit, the electrons
cycle back from ferrodoxin (Fd) to the cytochrome
complex and from there continue to a P700 chlorophyll
in the PSI reaction center complex. There is no
production of NADPH and no release of oxygen. It
does, however, generate ATP through captured energy
from the flow of electrons chemiosmosis. The last
reduced electron carrier (plastocyanin) passes the
electrons to the electron-deficient chlorophyll, allowing
the reactions to start again (Sadava et al., 2009).
These occur species that possess both
photosystems, as well as in several groups of
photosynthetic bacteria known to lack PSII (Sadava et
al., 2009).

SLIDE 14: Photophosphorylation


Photophosphorylation in the chloroplast is
similar to oxidative phosphorylation that occurs in the
mitochondrion. Both processes utilize proton pumps
that create a chemiosmotic gradient wherein [H+] is
greater in the intermembrane space and thylakoid space.
Protons from the higher concentration will then diffuse
into the matrix or the stroma through the ATP synthase.
This will trigger the formation of ATP from ADP and P i
at the ATPase (F1) region of the ATP synthase.
The difference between the two ATP
production processes is that while NADPH used in
oxidative phosphorylation is from glycolysis and citric
acid cycle, NADPH used in photophosphorylation is a
product of the light-dependent reactions.

SLIDE 15: How light energy is transformed and


transferred in the chloroplast to be used as energy has
been continuously discussed in the paper. However, it is
important to take note that, the step involving the
NADP+ reductase takes place on the stromal side of the
thylakoid membrane. The uptake of a proton by NADP+
further contributes to the pH gradient across the
thylakoid membrane.
The transport of electrons from water to
NADP+ generated a pH gradient across the thylakoid
membrane. This proton motive force is used to drive the
synthesis of ATP. The synthesis of ATP in the
chloroplast is nearly identical with ATP synthesis in the
mitochondrian. The pH gradient generated between the
stroma and the thylakoid lumen is possible because the
thylakoid membrane is impermeable to protons. When
the chloroplast is illuminated the thylakoid lumen
becomes markedly acidic. The transmembrane electrical
potential is not a significant factor in the proton motive
force in the chloroplast because the thylakoid membrane
is permeable to Cl- and Mg2+. Because of this
permeability, the thylakoid lumen remains electrically
neutral while the pH gradient is generated (Russell et
al., 2014).
The ATP synthase of the chloroplast is called
the CF1-CF0 complex where C stands for chloroplast
and F1 and F0 relate to the homologous ATP synthase
of the mitochondria. The mitochondrial and the
chloroplast ATP synthase are essentially identical with
similar subunits and subunit stoichiometries. The
catalytic subunit is the subunit of CF1. The CF1
complex lies in the stroma. The CF0 complex channels
protons from the thylakoid lumen to the stroma driving
rotation of the 12 c subunits which in turn drives ATP
synthesis. The ATP formed is released into the stroma
where it is needed for the dark reactions (Calvin Cycle)
of photosynthesis (Raven et al., 2005).

APOLONIO, CARANGIAN, SANCHEZ & TIGLAO

BIO 150 LEC 2


stroma. Starch is a large polymer of glucose that serves
as a carbohydrate reserve. The production of starch is
regulated so that it is produced and stored as large
grains in the chloroplast stroma during periods of excess
photosynthetic capacity. This occurs through reactions
in the stroma that are the reverse of those in glycolysis.
At night the starch is broken down to help support the
metabolic needs of the plant.

SLIDE 16: The Carbon Fixation Cycle


In the figure, the metabolic pathway that
produces ribulose 1,5-bisphosphate requires both
NADPH and ATP in the carbon-fixation cycle (Calvin
cycle). It starts when 3 molecules of CO2 are fixed by
ribulose bisphosphate carboxylase to produce 6
molecules of 3-phosphoglycerate (containing 6 3 = 18
carbon atoms in all: 3 from the CO2 and 15 from
ribulose 1,5-bisphosphate). The 18 carbon atoms then
undergo a cycle of reactions that regenerates the 3
molecules of ribulose 1,5-bisphosphate used in the
initial carbon-fixation step (containing 3 5 = 15
carbon atoms). This leaves 1 molecule of
glyceraldehyde 3-phosphate (3 carbon atoms) as the net
gain.
A total of 3 molecules of ATP and 2 molecules
of NADPH are consumed for each CO2 molecule
converted into carbohydrate. The net equation is:

Thus, both phosphate-bond energy (as ATP)


and reducing power (as NADPH) are required for the
formation of organic molecules from CO2 and H2O.
Much of the glyceraldehyde 3-phosphate
produced in chloroplasts by the carbon-fixation cycle is
exported to the cytosol where it can be converted into
fructose 6-phosphate and glucose 1-phosphate by the
reversal of several reactions in glycolysis. The glucose
1-phosphate is then converted to the sugar nucleotide
UDP-glucose, and this combines with the fructose 6phosphate to form sucrose phosphate, the immediate
precursor of the disaccharide sucrose. Sucrose is the
major form in which sugar is transported between plant
cells and is exported from the leaves via vascular
bundles providing the carbohydrate required by the rest
of the plant.
Most of the glyceraldehyde 3-phosphate that
remains in the chloroplast is converted to starch in the

Slide 17: Inside plant cells, the enzyme ribulose


bisphosphate carboxylase oxygenase (rubisco), takes
carbon dioxide and attaches it to ribulose 1,5bisphosphate, a short sugar chain with five carbon
atoms. Rubisco then clips the lengthened chain into two
identical phosphoglycerate pieces, each with three
carbon atoms (Berman et al., 2000).
Phosphoglycerates are familiar molecules in
the cell, and they are used in a variety of cell
metabolism pathways. Most of the phosophoglycerate
made by rubisco are recycled to build more ribulose
bisphosphate, to fuel carbon fixation. But one out of
every six molecules is skimmed off and used as food for
the plant, or stored away in the form of starch for later
use (Berman et al., 2000).

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BIO 150 LEC 2

REFERENCES
Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., ... & Bourne, P. E. (2000). The protein
data bank. Nucleic acids research, 28(1), 235-242.
Buchanan, B., Gruissem, W., & Jones, R. 2015. Biochemistry and Molecular Biology of Plants (2nd ed.). New York:
John Wiley & Sons.
McGraw
Hill
Education.
(2007).
Photosynthesis.
Retrieved
November
http://www.mhhe.com/biosci/genbio/raven6b/graphics/raven06b/other/raven06b_10.pdf

3,

2016

from

Miles, B. (2003). Photosystems I and II. Lecture presented in TX, College Station. Retrieved November 4, 2016, from
https://www.tamu.edu/faculty/bmiles/lectures/photosystems.pdf
Ort, D. R., & Yocum, C. F. (Eds.). (1996). Oxygenic photosynthesis: the light reactions (Vol. 4). Springer Science &
Business Media.
Raven P., Evert, R., & Eichhorn S. 2005. Biology of Plants, (7th ed.). New York: W. H. Freeman and Company.
Russell, P., Herz, P., & Mcmillan, B. 2014. Biology: the dynamic science (3rd ed.). Belmont, CA : Brooks/Cole,
Cengage Learning.
Sadava, D. E., Hillis, D. M., Heller, H. C., & Berenbaum, M. (2009). Life: the science of biology (Vol. 2). Macmillan.
Speer,
B. (1995, July 4).
Photosynthetic Pigments.
http://www.ucmp.berkeley.edu/glossary/gloss3/pigments.html

Retrieved

November

3,

2016,

from

Taiz, L., Zeiger, E., Mller, I. M., & Murphy, A. (2015). Plant physiology and development. Sinauer Associates,
Incorporated.
University of California Museum of Paleontology. Photosynthetic Pigments. Accessed on November 3, 2016. Accessed
from http://www.ucmp.berkeley.edu/glossary/gloss3/pigments.html
University of California Santa Barbara. Why is the chlorophyll in plants green or even red, orange, or brown? Accessed
on November 3, 2016. Accessed from http://scienceline.ucsb.edu/getkey.php?key=1110

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