Bioenergetics is the subject of a field of biochemistry that concerns energy flow through living systems.

This is an active area of biological research that includes the study of thousands of different cellular processes such as cellular respiration and the many other metabolic processes that can lead to production and utilization of energy in forms such as ATP molecules. Content:

1.Overview 2 Types of Reactions 3 Chemiosmotic theory 4 References 5 Additional reading

Overview
Bioenergetics is the part of biochemistry concerned with the energy involved in making and breaking of chemical bonds in the molecules found in biological organisms. Growth, development and metabolism are some of the central phenomena in the study of biological organisms. The role of energy is fundamental to such biological processes. The ability to harness energy from a variety of metabolic pathways is a property of all living organisms. Life is dependent on energy transformations; living organisms survive because of exchange of energy within and without. In a living organism, chemical bonds are broken and made as part of the exchange and transformation of energy. Energy is available for work (such as mechanical work) or for other processes (such as chemical synthesis and anabolic processes in growth), when weak bonds are broken and stronger bonds are made. The production of stronger bonds allows release of usable energy. Living organisms obtain energy from organic and inorganic materials. For example, lithotrophs can oxidize minerals such as nitrates or forms of sulfur, such as elemental

sulfur, sulfites, and hydrogen sulfide to produce ATP. In photosynthesis,autotrophs can produce ATP using light energy. Heterotrophs must consume organic compounds. These are mostly carbohydrates, fats, and proteins. The amount of energy actually obtained by the organism is lower than the amount present in the food; there are losses in digestion, metabolism, and thermogenesis. The materials are generally combined with oxygen to release energy, although some can also be oxidized anaerobically by various organisms. The bonds holding the molecules of nutrients together and the bonds holding molecules of free oxygen together are all relatively weak compared with the chemical bonds holding carbon dioxide and water together. The utilization of these materials is a form of slow combustion. The materials are oxidized slowly enough that the organisms do not actually produce fire. The oxidation releases energy because stronger bonds have been formed. This net energy may evolve as heat, or some of which may be used by the organism for other purposes, such as breaking other bonds to do chemistry. Living organisms produce ATP from energy sources via oxidative phosphorylation. The terminal phosphate bonds of ATP are relatively weak compared with the stronger bonds formed when ATP is broken down to adenosine monophosphate and phosphate, dissolved in water. Here it is the energy of hydration that results in energy release. This hydrolysis of ATP is used as a battery to store energy in cells, for intermediate metabolism. Utilization of chemical energy from such molecular bond rearrangement powers biological processes in every biological organism.

Types of Reactions

Exergonic is a spontaneous reaction that releases energy. It is thermodynamically favored. On the course of a reaction, energy needs to be put in, this activation energy drives the reactants from a stable state to a highly energetic unstable configuration. These reactants are usually complex molecules that are broken into simpler products. The entire reaction is usually catabolic. The release of energy, also called free energy is a - G because energy is lost from the bonds formed by the products. Endergonic is an anabolic reaction that consumes energy. It has a +G because energy is required to break bonds.

The free energy ( G) gained or lost in a reaction can be calculated: G= H - T S. Also, G = G' + 2.303RTlog([P]/[R]) where
o o o o

R is the gas constant, 1.987 cal/mol T is temperature in Kelvin K = 273 + C P is Products R is the reactants

The Free Energy Concept:

The free energy change ( G) of a reaction determines its spontaneity. The free energy change ( G), and its relation to equilibrium constant, are discussed on p. 57-59 of Biochemistry 3rd Edition by Voet & Voet. A reaction is spontaneous if G is negative (if the free energy of the products is less than the free energy of the reactants). G = change in free energy, Go' = standard free energy change (with 1 M reactants and products, at pH 7), R = gas constant, T = absolute temperature. Note that the standard free energy change ( Go') of a reaction may be positive, for example, and the actual free energy change ( G) negative, depending on cellular concentrations of reactants and products. Many reactions for which Go' is positive are spontaneous because other reactions cause depletion of products or maintenance of high substrate concentrations.

At equilibrium, G equals zero. Solving for Go' yields the relationship at left. K'eq, the ratio [C][D]/[A][B] at equilibrium, is called the equilibrium constant. An equilibrium constant greater than one (more products than reactants at equilibrium) indicates a spontaneous reaction (negative G'). A spontaneous reaction may drive a non-spontaneous reaction. Free energy changes of coupled reactions are additive.

Examples of different types of coupling: A. Some enzyme-catalyzed reactions are interpretable as two coupled half-reactions, one spontaneous and the other non-spontaneous. At the enzyme active site, the coupled reaction is kinetically facilitated, while the individual half-reactions are prevented. The

free energy changes of the half-reactions may be summed, to yield the free energy of the coupled reaction. For example, in the reaction catalyzed by the Glycolysis enzyme Hexokinase, the two half-reactions are:

ATP + H2O ADP + Pi .................. Go' = kJoules/mol 31 o Pi + glucose glucose-6-P + H2O ... G ' = +14 kJoules/mol

Coupled reaction: ATP + glucose ADP + glucose-6-P .. Go' = kJoules/mol 17 The structure of the enzyme active site, from which water is excluded, prevents the individual hydrolytic reactions, while favoring the coupled reaction. B. Two separate enzyme-catalyzed reactions occurring in the same cellular compartment, one spontaneous and the other non-spontaneous, may be coupled by a common intermediate (reactant or product). A hypothetical, but typical, example involving pyrophosphate:

enzyme 1: A + ATP B + AMP + PPi .... Go' = +15 kJ/mol enzyme 2: PPi + H2O 2 Pi .................... Go' = 33 kJ/mol

Overall: A + ATP + H2O B + AMP + 2Pi ... Go' = 18 kJ/mol

"High Energy" Bonds

The structure of ATP is shown below at right. Anhydride bonds (in red) link the terminal phosphates. Phosphoanhydride bonds (formed by splitting out water between two phosphoric acids or between a carboxylic acid and a phosphoric acid) tend to have a large negative G of hydrolysis, and are thus said to be "high energy" bonds. It is important to realize that the bond energy is not necessarily high, just the free energy of hydrolysis. "High energy" bonds are often represented by the "~" symbol (squiggle), with ~P representing a phosphate group with a high free energy of hydrolysis.

Compounds with "high energy" bonds are said to have high group transfer potential. For example, Pi may be spontaneously removed from ATP for transfer to another compound (e.g., to a hydroxyl group on glucose). Potentially two "high energy" bonds can be cleaved, as two phosphates are released by hydrolysis from ATP (adenosine triphosphate), yielding ADP (adenosine diphosphate), and ultimately AMP (adenosine monophosphate). This may be represented as follows (omitting waters of hydrolysis):

AMP~P~P AMP~P + Pi (ATP ADP + Pi) AMP~P AMP + Pi (ADP AMP + Pi)

Alternatively, as discussed above:

AMP~P~P AMP + P~Pi P~P 2 Pi

(ATP AMP + PPi)

ATP often serves as an energy source. Hydrolytic cleavage of one or both of the "high energy" bonds of ATP is coupled to an energy-requiring (non-spontaneous) reaction, as in the examples presented above. AMP functions as an energy sensor and regulator of metabolism. When ATP production does not keep up with needs, a higher portion of a cell's adenine nucleotide pool is in the form of AMP. AMP then stimulates metabolic pathways that produce ATP.

Some examples of this role involve direct allosteric activation of pathway enzymes by AMP. (E.g., activation of the Glycogen Phosphorylase enzyme by AMP will be discussed later.) Some regulatory effects of AMP are mediated by the enzyme AMP-Activated Protein Kinase.

Phosphocreatine (also called creatine phosphate), another compound with a "high energy" phosphate linkage, is used in nerve and muscle cells for storage of ~P bonds. Creatine Kinase catalyzes: phosphocreatine + ADP ATP + creatine This is a reversible reaction, though the equilibrium

constant slightly favors phosphocreatine formation. Phosphocreatine is produced when ATP levels are high. When ATP is depleted during exercise in muscle, phosphate is transferred from phosphocreatine to ADP, to replenish ATP. Phosphoenolpyruvate (PEP), involved in production of ATP in Glycolysis, has a larger negative G of phosphate hydrolysis than ATP. Removal of phosphate from the ester linkage in PEP is spontaneous because the enol product spontaneously converts to a ketone. :

ATP has special roles in energy coupling and phosphate transfer. The free energy of hydrolysis of phosphate from ATP is intermediate among the examples listed in the table below. ATP can thus act as a phosphate donor, and ATP can be synthesized by transfer of phosphate from other compounds, such as phosphoenolpyruvate (PEP). Compound Phosphoenolpyruvate (PEP) Phosphocreatine Pyrophosphate ATP (to ADP) Glucose-6-phosphate Glycerol-3-phosphate Go' of phosphate hydrolysis (kJ/mol) 61.9 43.1 33.5 30.5 13.8 9.2

Some other "high energy" bonds: A thioester forms between a carboxylic acid and a thiol (SH) group, e.g., the thiol of coenzyme A (abbreviated CoA-SH). Thioesters are "high energy" linkages. In contrast to phosphate esters, thioesters have a large negative G of hydrolysis. The thiol of coenzyme A can react with a carboxyl group of acetic acid (yielding acetylCoA) or a fatty acid (yielding fatty acyl-CoA). The spontaneity of thioester cleavage is essential to the role of coenzyme A as an acyl group carrier. Like ATP, acyl-coenzyme A has a high group transfer potential. Coenzyme A includes mercaptoethylamine, in amide linkage to the carboxyl group of the B vitamin pantothenate. The hydroxyl of pantothenate is in ester linkage to a phosphate of ADP-3'-phosphate. The functional group is the thiol (SH) of mercaptoethylamine.

Oxidation & reduction :The evolution of photosynthesis, and the generation of the
oxygen that is now plentiful in our environment, allowed development of metabolic pathways that derive energy from transfer of electrons from various reductants ultimately to molecular oxygen. Oxidation of an iron atom involves loss of an electron (to some acceptor atom): Fe++ (reduced) Fe+++ (oxidized) + eFor a carbon compound, increased oxidation means increased number of C-O bonds. Since electrons in a CO bond are associated more with the oxygen, the C becomes relatively electron deficient as you go from hydrocarbon to CO2. Oxidation of carbon is spontaneous (energy yielding). Two important electron carriers in metabolism are NAD+ and FAD. NAD+ (Nicotinamide Adenine Dinucleotide) functions as an electron acceptor in catabolic pathways. The nicotinamide ring of NAD+, which is derived from the vitamin niacin, accepts 2 eand one H+ (a hydride) in going to the reduced state, as NAD+ becomes NADH. See also p. 461 & 555. NADP+/NADPH is similar, except for an additional phosphate esterified to a hydroxyl group on the adenosine ribose. NADPH functions as an electron donor in synthetic pathways.

The electron transfer reaction may be summarized as: NAD+ + 2 e + H+ NADH It may also be written as: NAD+ + 2 e + 2H+ NADH + H+ FAD (Flavin Adenine Dinucleotide) also functions as an electron acceptor. The portion of FAD that undergoes reduction/oxidation is the dimethylisoalloxazine ring, derived from the vitamin riboflavin. See p. 556.

FAD normally accepts 2 e and 2 H+ in going to its reduced state: FAD + 2 e- + 2 H+ FADH2

NAD+ is a coenzyme, that reversibly binds to enzymes. FAD is a prosthetic group, that usually remains tightly bound at the active site of an enzyme.

Electron transport chain

The electron transport chain in the mitochondrion is the site of oxidative phosphorylation in eukaryotes. The NADH and succinate generated in the citric acid cycle is oxidized, providing energy to power ATP synthase.

An electron transport chain couples a chemical reaction between an electron donor (such as NADH) and an electron acceptor (such as O2) to the transfer of H+ ions across a membrane, through a set of mediating biochemical reactions. These H+ ions are used to

produce adenosine triphosphate (ATP), the main energy intermediate in living organisms, as they move back across the membrane

Background
The electron transport chain is also called the ETC. An enzyme called ATP synthase catalyzes a reaction to generate ATP. The structure of this enzyme and its underlying genetic code is remarkably conserved in all known forms of life. ATP synthase is powered by a transmembrane electrochemical potential gradient usually in the form of a proton gradient. The function of the electron transport chain is to produce this gradient. In all living organisms, a series of redox reactions is used to produce a transmembrane electrochemical potential gradient.

Electron transport chains in mitochondria

The cells of almost all eukaryotes (animals, plants, fungi, algae, protozoa in other words, the living things except bacteria, archaea, and a few protists) contain intracellular organelles called mitochondria, which produce ATP. Energy sources such as glucose are initially metabolized in the cytoplasm. The products are imported into mitochondria. Mitochondria continue the process of catabolism using metabolic pathways including the Krebs cycle, fatty acid oxidation, and amino acid oxidation. The end result of these pathways is the production of two kinds of energy-rich electron donors, NADH and succinate. Electrons from these donors are passed through an electron transport chain to oxygen, which is reduced to water. This is a multi-step redox process that occurs on the mitochondrial inner membrane. The enzymes that catalyze these reactions have the remarkable ability to simultaneously create a proton gradient across the membrane, producing a thermodynamically unlikely high-energy state with the potential to do work. Although electron transport occurs with great efficiency, a small percentage of electrons are prematurely leaked to oxygen, resulting in the formation of the toxic free-radical superoxide. The similarity between intracellular mitochondria and free-living bacteria is striking. The known structural, functional, and DNA similarities between mitochondria and bacteria

provide strong evidence that mitochondria evolved from intracellular bacterial symbionts (see Endosymbiotic theory).

Mitochondrial redox carriers

Stylized representation of the ETC. Energy obtained through the transfer of electrons (black arrows) down the ETC is used to pump protons (red arrows) from the mitochondrial matrix into the intermembrane space, creating an electrochemical proton gradient across the mitochondrial inner membrane (IMM) called . This electrochemical proton gradient allows ATP synthase (ATP-ase) to use the flow of H+ through the enzyme back into the matrix to generate ATP from adenosine diphosphate (ADP) and inorganic phosphate. Complex I (NADH coenzyme Q reductase; labeled I) accepts electrons from the Krebs cycle electron carrier nicotinamide adenine dinucleotide (NADH), and passes them to coenzyme Q (ubiquinone; labeled UQ), which also receives electrons from complex II (succinate dehydrogenase; labeled II). UQ passes electrons to complex III (cytochrome bc1 complex; labeled III), which passes them to cytochrome c (cyt c). Cyt c passes electrons to Complex IV (cytochrome c oxidase; labeled IV), which uses the electrons and hydrogen ions to reduce molecular oxygen to water. Four membrane-bound complexes have been identified in mitochondria. Each is an extremely complex transmembrane structure that is embedded in the inner membrane. Three of them are proton pumps. The structures are electrically connected by lipidsoluble electron carriers and water-soluble electron carriers. The overall electron transport chain
NADH Complex I Q Complex III cytochrome c Complex IV Complex II O2

Complex I
Complex I (NADH dehydrogenase, also called NADH:ubiquinone oxidoreductase; EC 1.6.5.3) removes two electrons from NADH and transfers them to a lipid-soluble carrier, ubiquinone (Q). The reduced product, ubiquinol (QH2) is free to diffuse within the membrane. At the same time, Complex I moves four protons (H+) across the membrane, producing a proton gradient. Complex I is one of the main sites at which premature electron leakage to oxygen occurs, thus being one of main sites of production of a harmful free radical called superoxide. The pathway of electrons occurs as follows: NADH is oxidized to NAD+, reducing Flavin mononucleotide to FMNH2 in one twoelectron step. The next electron carrier is a Fe-S cluster, which can only accept one electron at a time to reduce the ferric ion into a ferrous ion. In a convenient manner,

FMNH2 can be oxidized in only two one-electron steps, through a semiquinone intermediate. The electron thus travels from the FMNH2 to the Fe-S cluster, then from the Fe-S cluster to the oxidized Q to give the free-radical (semiquinone) form of Q. This happens again to reduce the semiquinone form to the ubiquinol form, QH2. During this process, four protons are translocated across the inner mitochondrial membrane, from the matrix to the intermembrane space. This creates a proton gradient that will be later used to generate ATP through oxidative phosphorylation.

[Complex II
Complex II (succinate dehydrogenase; EC 1.3.5.1) is not a proton pump. It serves to funnel additional electrons into the quinone pool (Q) by removing electrons from succinate and transferring them (via FAD) to Q. Complex II consists of four protein subunits: SDHA,SDHB,SDHC, and SDHD. Other electron donors (e.g., fatty acids and glycerol 3-phosphate) also funnel electrons into Q (via FAD), again without producing a proton gradient.

Complex III
Complex III (cytochrome bc1 complex; EC 1.10.2.2) removes in a stepwise fashion two electrons from QH2 at the QO site and sequentially transfers them to two molecules of cytochrome c, a water-soluble electron carrier located within the intermembrane space. The two other electrons are sequentially passed across the protein to the Qi site where quinone part of ubiquinone is reduced to quinol. A proton gradient is formed because it takes 2 quinol (4H+4e-) oxidations at the Qo site to form one quinol (2H+2e-) at the Qi site. (in total 6 protons: 2 protons reduce quinone to quinol and 4 protons are released from 2 ubiquinol). The bc1 complex does NOT 'pump' protons, it helps build the proton gradient by an asymmetric absorption/release of protons. When electron transfer is hindered (by a high membrane potential, point mutations or respiratory inhibitors such as antimycin A), Complex III may leak electrons to oxygen resulting in the formation of superoxide, a highly-toxic species, which is thought to contribute to the pathology of a number of diseases, including aging.

Complex IV
Complex IV (cytochrome c oxidase; EC 1.9.3.1) removes four electrons from four molecules of cytochrome c and transfers them to molecular oxygen (O2), producing two molecules of water (H2O). At the same time, it moves four protons across the membrane, producing a proton gradient.

Coupling with oxidative phosphorylation

The chemiosmotic coupling hypothesis, as proposed by Nobel Prize in Chemistry winner Peter D. Mitchell, explains that the electron transport chain and oxidative phosphorylation are coupled by a proton gradient across the inner mitochondrial

membrane. The efflux of protons creates both a pH gradient and an electrochemical gradient. This proton gradient is used by the FOF1 ATP synthase complex to make ATP via oxidative phosphorylation. ATP synthase is sometimes regarded as complex V of the electron transport chain. The FO component of ATP synthase acts as an ion channel for return of protons back to mitochondrial matrix. During their return, the free energy produced during the generation of the oxidized forms of the electron carriers (NAD+ and Q) is released. This energy is used to drive ATP synthesis, catalyzed by the F1 component of the complex. Coupling with oxidative phosphorylation is a key step for ATP production. However, in certain cases, uncoupling may be biologically useful. The inner mitochondrial membrane of brown adipose tissue contains a large amount of thermogenin (an uncoupling protein), which acts as uncoupler by forming an alternative pathway for the flow of protons back to matrix. This results in consumption of energy in thermogenesis rather than ATP production. This may be useful in cases when heat production is required, for example in colds or during arise of hibernating animals. Synthetic uncouplers (e.g., 2,4dinitrophenol) also exist, and, at high doses, are lethal.

Summary
The mitochondrial electron transport chain removes electrons from an electron donor (NADH or QH2) and passes them to a terminal electron acceptor (O2) via a series of redox reactions. These reactions are coupled to the creation of a proton gradient across the mitochondrial inner membrane. There are three proton pumps: I, III, and IV. The resulting transmembrane proton gradient is used to make ATP via ATP synthase. The reactions catalyzed by Complex I and Complex III exist roughly at equilibrium. This means that these reactions are readily reversible, simply by increasing the concentration of the products relative to the concentration of the reactants (for example, by increasing the proton gradient). ATP synthase is also readily reversible. Thus ATP can be used to make a proton gradient, which in turn can be used to make NADH. This process of reverse electron transport is important in many prokaryotic electron transport chains.

Chemiosmotic theory
One of the major triumphs of bioenergetics is Peter D. Mitchell's chemiosmotic theory of how protons in aqueous solution function in the production of ATP in cell organelles such as mitochondria. Other cellular sources of ATP such as glycolysis were understood first, but such processes for direct coupling of enzyme activity to ATP production are not the major source of useful chemical energy in most cells. Chemiosmotic coupling is the major energy producing process in most cells, being utilized in chloroplasts and many single celled organisms in addition to mitochondria.

PHOTOSYNTHESIS:
Photosynthesis is a metabolic pathway that converts carbon dioxide into organic compounds, especially sugars, using the energy from sunlight. Photosynthesis occurs in plants, algae, and many species of Bacteria, but not in Archaea. Photosynthetic organisms are called photoautotrophs, but not all organisms that use light as a source of energy carry out photosynthesis, since photoheterotrophs use organic compounds, rather than carbon dioxide, as a source of carbon. In plants, algae and cyanobacteria photosynthesis uses carbon dioxide and water, releasing oxygen as a waste product.

Photosynthetic membranes and organelles

Chloroplast ultrastructure: 1. outer membrane 2. intermembrane space 3. inner membrane (1+2+3: envelope) 4. stroma (aqueous fluid) 5. thylakoid lumen (inside of thylakoid) 6. thylakoid membrane 7. granum (stack of thylakoids) 8. thylakoid (lamella) 9. starch 10. ribosome 11. plastidial DNA 12. plastoglobule (drop of lipids)

Main articles: Chloroplast and Thylakoid The proteins that gather light for photosynthesis are embedded within cell membranes. The simplest way these are arranged is in photosynthetic bacteria, where these proteins are held within the plasma membrane. However, this membrane may be tightly-folded into cylindrical sheets called thylakoids, or bunched up into round vesicles called intracytoplasmic membranes. These structures can fill most of the interior of a cell, giving the membrane a very large surface area and therefore increasing the amount of light that the bacteria can absorb. In plants and algae, photosynthesis takes place in organelles called chloroplasts. A chloroplast is contained by an envelope that consists of an inner and an outer phospholipid membrane. Between these two layers is the intermembrane space. A typical plant cell contains about 10 to 100 chloroplasts. Within the stroma are stacks of thylakoids, the sub-organelles which are the site of photosynthesis. The thylakoids are arranged in stacks called grana (singular: granum). A thylakoid has a flattened disk shape. Inside it is an empty area called the thylakoid space or lumen. The thylakoid membrane contains many integral and peripheral membrane proteins. The proteins complexes which contain special pigments absorbing light energy are called photosystems. Plants absorb light primarily using the pigment chlorophyll, which is the reason that most plants have a green color. Besides chlorophyll, plants also use pigments such as carotenes and xanthophylls. Algae also use chlorophyll, but various other pigments are present as phycocyanin, carotenes, and xanthophylls in green algae, phycoerythrin in red algae (rhodophytes) and fucoxanthol in brown algae and diatoms resulting in a wide variety of colors. These pigments are embedded in plants and algae in special antenna-proteins. In such proteins all the pigments are ordered to work well together. Such a protein is also called a light-harvesting complex.

Light reactions

Light-dependent reactions of photosynthesis at the thylakoid membrane In the light reactions, one molecule of the pigment chlorophyll absorbs one photon and loses one electron. This electron is passed to a modified form of chlorophyll called pheophytin, which passes the electron to a quinone molecule, allowing the start of a flow of electrons down an electron transport chain that leads to the ultimate reduction of NADP to NADPH. In addition, this creates a proton gradient across the chloroplast membrane; its dissipation is used by ATP synthase for the concomitant synthesis of ATP. The chlorophyll molecule regains the lost electron from a water molecule through a process called photolysis, which releases a dioxygen (O2) molecule. The overall equation for the light-dependent reactions under the conditions of non-cyclic electron flow in green plants is: 2 H2O + 2 NADP+ + 2 ADP + 2 Pi + light 2 NADPH + 2 H+ + 2 ATP + O2 Not all wavelengths of light can support photosynthesis. The photosynthetic action spectrum depends on the type of accessory pigments present. For example, in green plants, the action spectrum resembles the absorption spectrum for chlorophylls and carotenoids with peaks for violet-blue and red light. In red algae, the action spectrum overlaps with the absorption spectrum of phycobilins for blue-green light, which allows these algae to grow in deeper waters that filter out the longer wavelengths used by green plants. The non-absorbed part of the light spectrum is what gives photosynthetic

organisms their color (e.g., green plants, red algae, purple bacteria) and is the least effective for photosynthesis in the respective organisms.

Z scheme

A Photosystem: A light-harvesting cluster of photosynthetic pigments present in the thylakoid membrane of chloroplasts.

The "Z scheme" In plants, light-dependent reactions occur in the thylakoid membranes of the chloroplasts and use light energy to synthesize ATP and NADPH. The light-dependent reaction has two forms; cyclic and non-cyclic reaction. In the non-cyclic reaction, the photons are captured in the light-harvesting antenna complexes of photosystem II by chlorophyll and other accessory pigments .When a chlorophyll molecule at the core of the photosystem II reaction center obtains sufficient excitation energy from the adjacent antenna pigments, an electron is transferred to the primary electron-acceptor molecule, Pheophytin, through a process called Photoinduced charge separation. These electrons are shuttled through an electron transport chain, the so called Z-scheme shown in the diagram, that initially functions to generate a chemiosmotic potential across the membrane. An ATP synthase enzyme uses the chemiosmotic potential to make ATP during photophosphorylation, whereas NADPH is a product of the terminal redox reaction in the Z-scheme. The electron enters the Photosystem I molecule. The electron is excited due to the light absorbed by the photosystem. A second electron carrier accepts the electron, which again is passed down lowering energies of electron acceptors. The energy created by the electron acceptors is used to move hydrogen ions across the thylakoid membrane into the lumen. The electron is used to reduce the co-enzyme NADP, which has functions in the light-independent reaction. The cyclic reaction is similar to that of the non-cyclic, but differs in the form that it generates only ATP, and no reduced NADP (NADPH) is created. The cyclic reaction takes place only at photosystem I. Once the electron is displaced from the photosystem, the electron is passed down the electron acceptor molecules and returns back to photosystem I, from where it was emitted, hence the name cyclic reaction.

Water photolysis:
Photodissociation and Oxygen evolution: The NADPH is the main reducing agent in chloroplasts, providing a source of energetic electrons to other reactions. Its production leaves chlorophyll with a deficit of electrons (oxidized), which must be obtained from some other reducing agent. The excited electrons lost from chlorophyll in photosystem I are replaced from the electron transport chain by plastocyanin. However, since photosystem II includes the first steps of the Zscheme, an external source of electrons is required to reduce its oxidized chlorophyll a molecules. The source of electrons in green-plant and cyanobacterial photosynthesis is water. Two water molecules are oxidized by four successive charge-separation reactions by photosystem II to yield a molecule of diatomic oxygen and four hydrogen ions; the electron yielded in each step is transferred to a redox-active tyrosine residue that then reduces the photoxidized paired-chlorophyll a species called P680 that serves as the primary (light-driven) electron donor in the photosystem II reaction center. The oxidation of water is catalyzed in photosystem II by a redox-active structure that contains four manganese ions and a calcium ion; this oxygen-evolving complex binds two water molecules and stores the four oxidizing equivalents that are required to drive the water-

oxidizing reaction. Photosystem II is the only known biological enzyme that carries out this oxidation of water. The hydrogen ions contribute to the transmembrane chemiosmotic potential that leads to ATP synthesis. Oxygen is a waste product of lightdependent reactions, but the majority of organisms on Earth use oxygen for cellular respiration, including photosynthetic organisms.

Light-independent reactions
The Calvin Cycle
Main articles: Carbon fixation and Light-independent reaction In the Light-independent or dark reactions the enzyme RuBisCO captures CO2 from the atmosphere and in a process that requires the newly formed NADPH, called the CalvinBenson Cycle, releases three-carbon sugars, which are later combined to form sucrose and starch. The overall equation for the light-independent reactions in green plants is: 3 CO2 + 9 ATP + 6 NADPH + 6 H+ C3H6O3-phosphate + 9 ADP + 8 Pi + 6 NADP+ + 3 H2O

Overview of the Calvin cycle and carbon fixation To be more specific, carbon fixation produces an intermediate product, which is then converted to the final carbohydrate products. The carbon skeletons produced by photosynthesis are then variously used to form other organic compounds, such as the building material cellulose, as precursors for lipid and amino acid biosynthesis, or as a fuel in cellular respiration. The latter occurs not only in plants but also in animals when the energy from plants gets passed through a food chain.

The fixation or reduction of carbon dioxide is a process in which carbon dioxide combines with a five-carbon sugar, ribulose 1,5-bisphosphate (RuBP), to yield two molecules of a three-carbon compound, glycerate 3-phosphate (GP), also known as 3phosphoglycerate (PGA). GP, in the presence of ATP and NADPH from the lightdependent stages, is reduced to glyceraldehyde 3-phosphate (G3P). This product is also referred to as 3-phosphoglyceraldehyde (PGAL) or even as triose phosphate. Triose is a 3-carbon sugar (see carbohydrates). Most (5 out of 6 molecules) of the G3P produced is used to regenerate RuBP so the process can continue (see Calvin-Benson cycle). The 1 out of 6 molecules of the triose phosphates not "recycled" often condense to form hexose phosphates, which ultimately yield sucrose, starch and cellulose. The sugars produced during carbon metabolism yield carbon skeletons that can be used for other metabolic reactions like the production of amino acids and lipids.

C4 and C3 photosynthesis and CAM

Overview of C4 carbon fixation In hot and dry conditions, plants will close their stomata to prevent loss of water. Under these conditions, CO2 will decrease, and dioxygen gas, produced by the light reactions of photosynthesis, will increase in the leaves, causing an increase of photorespiration by the oxygenase activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and decrease in carbon fixation. Some plants have evolved mechanisms to increase the CO2 concentration in the leaves under these conditions.

C4 plants chemically fix carbon dioxide in the cells of the mesophyll by adding it to the three-carbon molecule phosphoenolpyruvate (PEP), a reaction catalyzed by an enzyme called PEP carboxylase and which creates the four-carbon organic acid, oxaloacetic acid. Oxaloacetic acid or malate synthesized by this process is then translocated to specialized bundle sheath cells where the enzyme, rubisco, and other Calvin cyle enzymes are located, and where CO2 released by decarboxylation of the four-carbon acids is then fixed by rubisco activity to the three-carbon sugar 3-Phosphoglyceric_acids. The physical separation of rubisco from the oxygen-generating light reactions reduces photorespiration and increases CO2 fixation and thus photosynthetic capacity of the leaf. C4 plants can produce more sugar than C3 plants in conditions of high light and temperature. Many important crop plants are C4 plants including maize, sorghum, sugarcane, and millet. Plants lacking PEP-carboxylase are called C3 plants because the primary carboxylation reaction, catalyzed by Rubiso, produces the three-carbon sugar 3-phosphoglyceric acids directly in the Calvin-Benson Cycle. CAM photosynthesis Xerophytes such as cacti and most succulents also use PEP carboxylase to capture carbon dioxide in a process called Crassulacean acid metabolism (CAM). In contrast to C4 metabolism, which physically separates the CO2 fixation to PEP from the Calvin cycle, CAM only temporally separates these two processes. CAM plants have a different leaf anatomy than C4 plants, and fix the CO2 at night, when their stomata are open. CAM plants store the CO2 mostly in the form of malic acid via carboxylation of phosphoenolpyruvate to oxaloacetate, which is then reduced to malate. Decarboxylation of malate during the day releases CO2 inside the leaves thus allowing carbon fixation to 3-phosphoglycerate by rubisco.