A photosynthetic reaction center is a complex of several proteins, pigments and other co-factors

assembled together to execute the primary energy conversion reactions of photosynthesis. Molecular
excitations, either originating directly from sunlight or transferred as excitation energy via light-
harvesting antenna systems, give rise to electron transfer reactions along a series of protein-bound
co-factors. These co-factors are light-absorbing molecules (also named chromophores or pigments)
such as chlorophyll and pheophytin, as well as quinones. The energy of the photon is used to
promote an electron to a higher molecular energy level of a pigment. The free energy created is then
used to reduce a chain of nearby electron acceptors, which have subsequently lowered redox-
potentials. These electron transfer steps are the initial phase of a series of energy conversion
reactions, ultimately resulting in the production of chemical energy during photosynthesis.

Reaction centers are present in all green plants, algae, and many bacteria. Although these species are
separated by billions of years of evolution, the reaction centers are homologous for all
photosynthetic species. In contrast, a large variety in light-harvesting complexes exist between the
photosynthetic species. Green plants and algae have two different types of reaction centers that are
part of larger supercomplexes known as photosystem I and photosystem II. The structures of these
supercomplexes are large, involving multiple light-harvesting complexes. The reaction center found
in Rhodopseudomonas bacteria is currently best understood, since it was the first reaction center of
known structure and has fewer polypeptide chains than the examples in green plants.[1]

A reaction center is laid out in such a way that it captures the energy of a photon using pigment
molecules and turns it into a usable form. Once the light energy has been absorbed directly by the
pigment molecules, or passed to them by resonance transfer from a surrounding light-harvesting
complex, they release two electrons into an electron transport chain.

Light is made up of small bundles of energy called photons. If a photon with the right amount of
energy hits an electron, it will raise the electron to a higher energy level.[2] Electrons are most stable
at their lowest energy level, what is also called its ground state. In this state, the electron is in the
orbit that has the least amount of energy.[3] Electrons in higher energy levels can return to ground
state in a manner analogous to a ball falling down a staircase. In doing so, the electrons release
energy. This is the process that is exploited by a photosynthetic reaction center.

When an electron rises to a higher energy level, increase in the reduction potential of the molecule in
which the electron resides occurs. This means that the molecule has a greater tendency to donate
electrons, the key to the conversion of light energy to chemical energy. In green plants, the electron
transport chain that follows has many electron acceptors including pheophytin, quinone,
plastoquinone, cytochrome bf, and ferredoxin, which result in the reduced molecule NADPH. The
passage of the electron through the electron transport chain also results in the pumping of protons
(hydrogen ions) from the chloroplast's stroma into the lumen, resulting in a proton gradient across
the thylakoid membrane that can be used to synthesise ATP using ATP synthase. Both the ATP and
NADPH are used in the Calvin cycle to fix carbon dioxide into triose sugars.

Bacterial photosynthetic reaction centre.

The bacterial photosynthetic reaction center has been an important model to understand the structure
and chemistry of the biological process of capturing light energy. In the 1960s, Roderick Clayton
was the first to purify the reaction center complex from purple bacteria. However, the first crystal
structure was determined in 1982 by Hartmut Michel, Johann Deisenhofer and Robert Huber for
which they shared the Nobel Prize in 1988. This was also significant, since it was the first structure
for any membrane protein complex.

Four different subunits were found to be important for the function of the photosynthetic reaction
center. The L and M subunits, shown in blue and purple in the image of the structure, both span the
plasma membrane. They are structurally similar to one another, both having 5 transmembrane
polypeptide helices.[4] Four bacteriochlorophyll b (BChl-b) molecules, two bacteriophaeophytin b
molecules (BPh) molecules, two quinones (QA and QB), and a ferrous ion are associated with the L
and M subunits. The H subunit, shown in gold, lies on the cytoplasmic side of the plasma membrane.
A cytochrome subunit, here not shown, contains four c-type hemes and is located on the periplasmic
surface (outer) of the membrane. The latter sub-unit is not a general structural motif in
photosynthetic bacteria. The L and M subunits bind the functional and light-interacting cofactors,
shown here in green.

Reaction centers from different bacterial species may contain slightly altered bacterio-chlorophyll
and bacterio-pheophytin chromophores as functional co-factors. These alterations cause shifts in the
color of light that can be absorbed, thus creating specific niches for photosynthesis. The reaction
center contains two pigments that serve to collect and transfer the energy from photon absorption:
BChl and Bph. BChl roughly resembles the chlorophyll molecule found in green plants, but, due to
minor structural differences, its peak absorption wavelength is shifted into the infrared, with
wavelengths as long as 1000 nm. Bph has the same structure as BChl, but the central magnesium ion
is replaced by two protons. This alteration causes both an absorbance maximum shift and a lowered
redox-potential.

[edit] Mechanism

The light reaction

The process starts when light is absorbed by two BChl molecules that lie near the periplasmic side of
the membrane. This pair of chlorophyll molecules, often called the "special pair", absorbs photons
between 870 nm and 960 nm, depending on the species and, thus, is called P870 (for the species
rhodobacter sphaeroides) or P960 (for rhodopseudomonas viridis), with P standing for "pigment").
Once P absorbs a photon, it ejects an electron, which is transferred through another molecule of Bchl
to the BPh in the L subunit. This initial charge separation yields a positive charge on P and a
negative charge on the BPh. This process takes place in 10 picoseconds (10-11 seconds).[1]

The charges on the specialpair + and the BPh- could undergo charge recombination in this state. This
would waste the high-energy electron and convert the absorbed light energy in to heat. Several
factors of the reaction center structure serve to prevent this. First, the transfer of an electron from
BPh- to P960+ is relatively slow compared to two other redox reactions in the reaction center. The
faster reactions involve the transfer of an electron from BPh- (BPh- is oxidised to BPh) to the
electron acceptor quinone (QA), and the transfer of an electron to P960+ (P960+ is reduced to P960)
from a heme in the cytochrome subunit above the reaction center.
The high-energy electron that resides on the tightly bound quinone molecule Q A is transferred to an
exchangeable quinone molecule QB. This molecule is loosely associated with the protein and is fairly
easy to detach. Two of the high-energy electrons are required to fully reduce Q B to QH2, taking up
two protons from the cytoplasm in the process. The reduced quinone QH2 diffuses through the
membrane to another protein complex (cytochrome bc1-complex) where it is oxidised. In the process
the reducing power of the QH2 is used to pump protons across the membrane to the periplasmic
space. The electrons from the cytochrome bc1-complex are then transferred through a soluble
cytochrome c intermediate, called cytochrome c2, in the periplasm to the cytochrome subunit. Thus,
the flow of electrons in this system is cyclical.

In 1772, the chemist Joseph Priestley carried out a series of experiments relating to the gases
involved in respiration and combustion. In his first experiment, he lit a candle and placed it under an
upturned jar. After a short period of time, the candle burned out. He carried out a similar experiment
with a mouse in the confined space of the burning candle. He found that the mouse died a short time
after the candle had been extinguished. However, he could revivify the foul air by placing green
plants in the area and exposing them to light. Priestley's observations were some of the first
experiments that demonstrated the activity of a photosynthetic reaction center.

In 1779, Jan Ingenhousz carried out more than 500 experiments spread out over 4 months in an
attempt to understand what was really going on. He wrote up his discoveries in a book entitled
Experiments upon Vegetables. Ingenhousz took green plants and immersed them in water inside a
transparent tank. He observed many bubbles rising from the surface of the leaves whenever the
plants were exposed to light. Ingenhousz collected the gas that was given off by the plants and
performed several different tests in attempt to determine what the gas was. The test that finally
revealed the identity of the gas was placing a smouldering taper into the gas sample and having it
relight. This test proved it was oxygen, or, as Joseph Priestley had called it, 'de-phlogisticated air'.

In 1932, Professor Robert Emerson and an undergraduate student, William Arnold, used a repetitive
flash technique to precisely measure small quantities of oxygen evolved by chlorophyll in the algae
Chlorella. Their experiment proved the existence of a photosynthetic unit. Gaffron and Wohl later
interpreted the experiment and realized that the light absorbed by the photosynthetic unit was
transferred.[5] This reaction occurs at the reaction centre of photosystem II and takes place in
cyanobacteria, algae and green plants.[6]

[edit] Photosystem II

Cyanobacteria photosystem II, Monomer, PDB 2AXT.

Photosystem II is the photosystem that generates the two electrons that will eventually reduce
NADP+ in Ferredoxin-NADP-reduktase. Photosystem II is present on the thylakoid membranes
inside chloroplasts, the site of photosynthesis in green plants.[7] The structure of Photosystem II is
remarkably similar to the bacterial reaction center, and it is theorized that they share a common
ancestor.
The core of photosystem II consists of two subunits referred to as D1 and D2. These two subunits
are similar to the L and M subunits present in the bacterial reaction center. Photosystem II differs
from the bacterial reaction center in that it has many additional subunits that bind additional
chlorophylls to increase efficiency. The overall reaction catalyzed by photosystem II is:

Q represents plastoquinone, the oxidized form of Q. QH2 represents plastoquinol, the reduced form
of Q. This process of reducing quinone is comparable to that which takes place in the bacterial
reaction center. Photosystem II obtains electrons by oxidizing water in a process called photolysis.
Molecular oxygen is a byproduct of this process, and it is this reaction that supplies the atmosphere
with oxygen. The fact that the oxygen from green plants originated from water was first deduced by
the Canadian-born American biochemist Martin David Kamen. He used a natural, stable isotope of
oxygen, O18 to trace the path of the oxygen, from water to gaseous molecular oxygen. This reaction
is catalyzed by a reactive center in photosystem II containing four manganese ions.

The reaction begins with the excitation of a pair of chlorophyll molecules similar to those in the
bacterial reaction center. Due to the presence of chlorophyll a, as opposed to bacteriochlorophyll,
photosystem II absorbs light at a shorter wavelength. The pair of chlorophyll molecules at the
reaction center are often referred to as P680.[1] When the photon has been absorbed, the resulting
high-energy electron is transferred to a nearby pheophytin molecule. This is above and to the right of
the pair on the diagram and is coloured grey. The electron travels from the pheophytin molecule
through two plastoquinone molecules, the first tightly bound, the second loosely bound. The tightly
bound molecule is shown above the pheophytin molecule and is coloured red. The loosely bound
molecule is to the left of this and is also coloured red. This flow of electrons is similar to that of the
bacterial reaction center. Two electrons are required to fully reduce the loosely bound plastoquinone
molecule to QH2 as well as the uptake of two protons.

The difference between photosystem II and the bacterial reaction center is the source of the electron
that neutralizes the pair of chlorophyll a molecules. In the bacterial reaction center, the electron is
obtained from a reduced compound heme group in a cytochrome subunit or from a water-soluble
cytochrome-c protein.

Once photoinduced charge separation has taken place, the P680 molecule carries a positive charge.
P680 is a very strong oxidant and extracts electrons from two water molecules that are bound at the
manganese center directly below the pair. This center, below and to the left of the pair in the
diagram, contains four manganese ions, a calcium ion, a chloride ion, and a tyrosine residue.
Manganese is used because it is capable of existing in four oxidation states: Mn2+, Mn3+, Mn4+ and
Mn5+. Manganese also forms strong bonds with oxygen-containing molecules such as water.

Every time the P680 absorbs a photon, it emits an electron, gaining a positive charge. This charge is
neutralized by the extraction of an electron from the manganese center, which sits directly below it.
The process of oxidizing two molecules of water requires four electrons. The water molecules that
are oxidized in the manganese center are the source of the electrons that reduce the two molecules of
Q to QH2. To date, this water-splitting catalytic center cannot be reproduced by any man-made
catalyst.

[edit] Photosystem I

After the electron has left photosystem II it is transferred to a cytochrome b6f complex and then to
plastocyanin, a blue copper protein and electron carrier. The plastocyanin complex carries the
electron that will neutralize the pair in the next reaction center, photosystem I.

As with photosystem II and the bacterial reaction center, a pair of chlorophyll a molecules initiates
photoinduced charge separation. This pair is referred to as P700. 700 Is a reference to the
wavelength at which the chlorophyll molecules absorb light maximally. The P700 lies in the center
of the protein. Once photoinduced charge separation has been initiated, the electron travels down a
pathway through a chlorophyll α molecule situated directly above the P700, through a quinone
molecule situated directly above that, through three 4Fe-4S clusters, and finally to an
interchangeable ferredoxin complex. Ferredoxin is a soluble protein containing a 2Fe-2S cluster
coordinated by four cysteine residues. The positive charge left on the P700 is neutralized by the
transfer of an electron from plastocyanin. Thus the overall reaction catalyzed by photosystem I is:

The cooperation between photosystems I and II creates an electron flow from H2O to NADP+. This
pathway is called the 'Z-scheme' because the redox diagram from P680 to P700 resembles the letter
z.[8]

Xanthophylls (originally phylloxanthins) are yellow pigments from the carotenoid group. The
name is from Greek xanthos (ξανθος, "yellow") + phyllon (φύλλον, "leaf"), due to their contribution
to the yellow band in early chromatography of leaf pigments. Their molecular structure is similar to
carotenes, but they have oxygen atoms. Thus, they are carotenoids but no longer carotenes.

Xanthophylls either contain hydroxyl groups and/or pairs of hydrogen atoms that are substituted by
oxygen atoms. For this reason they are more polar than the purely hydrocarbon carotenes. Due to
this difference, the carotenes travel further than xanthophylls in paper chromatography, since the
support paper is always hydrophillic.

Xanthophylls are found in the leaves of most plants, where they act to modulate light energy. The
xanthopylls found in the bodies of animals come from their food, and are ultimately derived from
plant sources, even in dietary animal products which contain them. For example, the yellow color of
chicken egg yolks, fat, and skin comes from ingested xanthophylls (primarily lutein, which is often
added to feed for this purpose). The yellow color of the human macula lutea (literally, yellow spot)
in the retina of the eye comes from the lutein and zeaxanthin it contains, both xanthophylls again
derived from the diet. These function in eye protection, but not directly in vision, since they cannot
be converted to retinal (also called retinaldehyde or vitamin A aldehyde).
The group of xanthophylls includes lutein, zeaxanthin, neoxanthin, violaxanthin, and α- and β-
cryptoxanthin. The latter compound is the only known xanthophyll to contain a beta-ionone ring, and
thus β-cryptoxanthin is the only xanthophyll which is known to possess pro-vitamin A activity for
mammals. Even then, it is a vitamin only for plant-eating species which possess the enzyme to make
retinal from those carotenoids which contain beta-ionone. Insects use 3-hydroxyretinal for visual
activities, which means that β-cryptoxanthin and other xanthophylls (such as lutein and zeaxanthin)
function as forms of visual "vitamin A" for them, but not carotenes. Squids use 4-hydroxyretinal,
which requires conversion of yet other xanthophylls.

Carotenoids are tetraterpenoid organic pigments that are naturally occurring in the chloroplasts and
chromoplasts of plants and some other photosynthetic organisms like algae, some types of fungus
some bacteria and at least one species of aphid. Carotenoids are generally not manufactured by
species in the animal kingdom, although one species of aphid is known to have acquired the genes
for synthesis of the carotenoid torulene from fungi, by the known phenomenon of horizontal gene
transfer.[1]

There are over 600 known carotenoids; they are split into two classes, xanthophylls (which contain
oxygen) and carotenes (which are purely hydrocarbons, and contain no oxygen). Carotenoids in
general absorb blue light. They serve two key roles in plants and algae: they absorb light energy for
use in photosynthesis, and they protect chlorophyll from photodamage.[2] In humans, four
carotenoids (beta-carotene, alpha-carotene, gamma-carotene, and beta-cryptoxanthin) have vitamin
A activity (meaning they can be converted to retinal), and these and other carotenoids can also act as
antioxidants. In the eye, certain other carotenoids (lutein and zeaxanthin) apparently act directly to
absorb damaging blue and near-ultraviolet light, in order to protect the macula lutea.

People consuming diets rich in carotenoids from natural foods, such as fruits and vegetables, are
healthier and have lower mortality from a number of chronic illnesses.[3] However, a recent meta-
analysis of 68 reliable antioxidant supplementation experiments involving a total of 232,606
individuals concluded that consuming additional β-carotene from supplements is unlikely to be
beneficial and may actually be harmful,[4] although this conclusion may be due to the inclusion of
studies involving smokers.[5] With the notable exception of Vietnam Gac and crude palm oil, most
carotenoid-rich fruits and vegetables are low in lipids. Since dietary lipids have been hypothesized to
be an important factor for carotenoid bioavailability, a 2005 study investigated whether addition of
avocado fruit or oil, as lipid sources, would enhance carotenoid absorption in humans. The study
found that the addition of both avocado fruit and oil significantly enhanced the subjects' absorption
of all carotenoids tested (α-carotene, β-carotene, lycopene, and lutein).[6]

Carotenoids belong to the category of tetraterpenoids (i.e. they contain 40 carbon atoms).
Structurally they are in the form of a polyene chain which is sometimes terminated by rings.

• Carotenoids with molecules containing oxygen, such as lutein and zeaxanthin, are known as
xanthophylls.
• The unoxygenated (oxygen free) carotenoids such as α-carotene, β-carotene and lycopene are
known as carotenes. Carotenes typically contain only carbon and hydrogen.
Probably the most well-known carotenoid is the one that gives this second group its name, carotene,
found in carrots (also apricots) and are responsible for their bright orange colour. Crude palm oil,
however, is the richest source of carotenoids in nature in terms of retinol (provitamin A) equivalent.
[7]
Vietnamese Gac fruit contains the highest known concentration of the carotenoid lycopene.

Their colour, ranging from pale yellow through bright orange to deep red, is directly linked to their
structure. Xanthophylls are often yellow, hence their class name. The double carbon-carbon bonds
interact with each other in a process called conjugation, which allows electrons in the molecule to
move freely across these areas of the molecule. As the number of double bonds increases, electrons
associated with conjugated systems have more room to move, and require less energy to change
states. This causes the range of energies of light absorbed by the molecule to decrease. As more
frequencies of light are absorbed from the short end of the visible spectrum, the compounds acquire
an increasingly red appearance.