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Photosystem2
Photosystems are functional and structural units of protein complexes involved in photosynthesis. Together they carry out the primary photochemistry of photosynthesis: the absorption of light and the transfer of energy and electrons. Photosystems are found in the thylakoid membranes of plants, algae, and cyanobacteria. These membranes are located inside the chloroplasts of plants and algae, and in the cytoplasmic membrane of photosynthetic bacteria. There are two kinds of photosystems: PSI and PSII. PSII will absorb red light, and PSI will absorb far-red light. Although photosynthetic activity will be detected when the photosystems are exposed to either red or far-red light, the photosynthetic activity will be the greatest when plants are exposed to both wavelengths of light. Studies have actually demonstrated that the two wavelengths together have a synergistic effect on the photosynthetic activity, rather than an additive one. Each photosystem has two parts: a reaction center, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thylakoid Membrane 3
Thylakoids are membrane-bound compartments inside chloroplasts and cyanobacteria. They are the site of the light-dependent reactions of photosynthesis. Thylakoids consist of a thylakoid membrane surrounding a thylakoid lumen. Chloroplast thylakoids frequently form stacks of disks referred to as grana (singular: granum). Grana are connected by intergranal/stromal thylakoids, which join granum stacks together as a single functional compartment. In thylakoid membranes, chlorophyll pigments are found in packets called quantasomes. Each quantasome contains 230 to 250 chlorophyll molecules. Etymology The word ''Thylakoid'' comes from the Greek word ''thylakos'' or ''θύλακος'', meaning "sac" or "pouch". Thus, ''thylakoid'' means "sac-like" or "pouch-like". Structure Thylakoids are membrane-bound structures embedded in the chloroplast stroma. A stack of thylakoids is called a granum and resembles a stack of coins. Membrane The thylakoid membrane is the site of the light- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Redox
Redox (reduction–oxidation, , ) is a type of chemical reaction in which the oxidation states of substrate (chemistry), substrate change. Oxidation is the loss of Electron, electrons or an increase in the oxidation state, while reduction is the gain of electrons or a decrease in the oxidation state. There are two classes of redox reactions: * ''Electron-transfer'' – Only one (usually) electron flows from the reducing agent to the oxidant. This type of redox reaction is often discussed in terms of redox couples and electrode potentials. * ''Atom transfer'' – An atom transfers from one substrate to another. For example, in the rusting of iron, the oxidation state of iron atoms increases as the iron converts to an oxide, and simultaneously the oxidation state of oxygen decreases as it accepts electrons released by the iron. Although oxidation reactions are commonly associated with the formation of oxides, other chemical species can serve the same function. In hydrogen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron–sulfur Cluster
Iron–sulfur clusters (or iron–sulphur clusters in British spelling) are molecular ensembles of iron and sulfide. They are most often discussed in the context of the biological role for iron–sulfur proteins, which are pervasive. Many Fe–S clusters are known in the area of organometallic chemistry and as precursors to synthetic analogues of the biological clusters (see Figure). It is believed that the last universal common ancestor had many iron-sulfur clusters. Organometallic clusters Organometallic Fe–S clusters include the sulfido carbonyls with the formula Fe2S2(CO)6, H2Fe3S(CO)9, and Fe3S2(CO)9. Compounds are also known that incorporate cyclopentadienyl ligands, such as (C5H5)4Fe4S4. Inorganic materials center, Structure of potassium dithioferrate, which features infinite chains of Fe(III) centers. Biological Fe–S clusters Iron–sulfur clusters occur in many biological systems, often as components of electron transfer proteins. The ferredoxin proteins a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carotenoids
Carotenoids (), also called tetraterpenoids, are yellow, orange, and red organic pigments that are produced by plants and algae, as well as several bacteria, and fungi. Carotenoids give the characteristic color to pumpkins, carrots, parsnips, corn, tomatoes, canaries, flamingos, salmon, lobster, shrimp, and daffodils. Carotenoids can be produced from fats and other basic organic metabolic building blocks by all these organisms. It is also produced by endosymbiotic bacteria in whiteflies. Carotenoids from the diet are stored in the fatty tissues of animals, and exclusively carnivorous animals obtain the compounds from animal fat. In the human diet, absorption of carotenoids is improved when consumed with fat in a meal. Cooking carotenoid-containing vegetables in oil and shredding the vegetable both increase carotenoid bioavailability. There are over 1,100 known carotenoids which can be further categorized into two classes, xanthophylls (which contain oxygen) and carote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pheophytin
Pheophytin or phaeophytin is a chemical compound that serves as the first electron carrier intermediate in the electron transfer pathway of Photosystem II (PS II) in plants, and the type II photosynthetic reaction center (RC P870) found in purple bacteria. In both PS II and RC P870, light drives electrons from the reaction center through pheophytin, which then passes the electrons to a quinone (QA) in RC P870 and RC P680. The overall mechanisms, roles, and purposes of the pheophytin molecules in the two transport chains are analogous to each other. Structure In biochemical terms, pheophytin is a chlorophyll molecule lacking a central Mg2+ ion. It can be produced from chlorophyll by treatment with a weak acid, producing a dark bluish waxy pigment. The probable etymology comes from this description, with ''pheo'' meaning ''dusky'' and ''phyt'' meaning ''vegetation''. [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Quinone
The quinones are a class of organic compounds that are formally "derived from aromatic compounds [such as benzene or naphthalene] by conversion of an even number of –CH= groups into –C(=O)– groups with any necessary rearrangement of double bonds, resulting in "a fully Conjugated system, conjugated cyclic diketone, dione structure". The archetypical member of the class is 1,4-benzoquinone or cyclohexadienedione, often called simply "quinone" (thus the name of the class). Other important examples are 1,2-benzoquinone (''ortho''-quinone), 1,4-naphthoquinone and anthraquinone, 9,10-anthraquinone. The name is derived from that of quinic acid (with the suffix "-one" indicating a ketone), since it is one of the compounds obtained upon oxidation of quinic acid. Quinic acid, like quinine is obtained from cinchona bark, called wikt:quinaquina, quinaquina in the indigenous languages of Peruvian tribes. Properties Quinones are oxidized derivatives of aromatic compounds and are often re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ferredoxin
Ferredoxins (from Latin ''ferrum'': iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium '' Clostridium pasteurianum''. Another redox protein, isolated from spinach chloroplasts, was termed "chloroplast ferredoxin". The chloroplast ferredoxin is involved in both cyclic and non-cyclic photophosphorylation reactions of photosynthesis. In non-cyclic photophosphorylation, ferredoxin is the last electron acceptor thus reducing the enzyme NADP+ reductase. It accepts electrons produced from sunlight- excited chlorophyll and transfers them to the enzyme ferredoxin: NADP+ oxidoreductase . Ferredoxins are small proteins containing iron and sulfur atoms organized as iron–sulfur clusters. These biological " capacitors" can ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nanometer
330px, Different lengths as in respect to the molecular scale. The nanometre (international spelling as used by the International Bureau of Weights and Measures; SI symbol: nm) or nanometer (American and British English spelling differences#-re, -er, American spelling) is a units of measurement, unit of length in the International System of Units (SI), equal to one billionth (short scale) of a metre () and to 1000 picometres. One nanometre can be expressed in scientific notation as , and as metres. History The nanometre was formerly known as the millimicrometre – or, more commonly, the millimicron for short – since it is of a micron (micrometre), and was often denoted by the symbol mμ or (more rarely and confusingly, since it logically should refer to a ''millionth'' of a micron) as μμ. Etymology The name combines the SI prefix ''nano-'' (from the Ancient Greek , ', "dwarf") with the parent unit name ''metre'' (from Greek , ', "unit of measurement"). ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
P680
P680, or photosystem II primary donor, is the reaction-center chlorophyll ''a'' molecular dimer associated with photosystem II in plants, algae, and cyanobacteria, and central to oxygenic photosynthesis. Etymology Its name is derived from the word “pigment” (P) and the presence of a major bleaching band centered around 680-685 nm in the flash-induced absorbance difference spectra of P680/ P680+•.Shigeru Itoh, S; Iwaki, M; Tomo, T; Satoh, K (1996). Dibromothymoquinone (DBMIB) replaces the function of QA at 77 K in the isolated photosystem II reaction center (Dl-D2-cytochrome 6559) complex: Difference spectrum of the P680+ (DBMIB") state. Plant Cell Physiol. 37(6): 833-839. Components The structure of P680 consists of a heterodimer of two distinct chlorophyll molecules, referred to as P and P. This “special pair” forms an excitonic dimer that functions as a single unit, excited by light energy as if they were a single molecule. Action and function Excitation ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photosystem II
Photosystem II (or water-plastoquinone oxidoreductase) is the first protein complex in the light-dependent reactions of oxygenic photosynthesis. It is located in the thylakoid membrane of plants, algae, and cyanobacteria. Within the photosystem, enzymes capture photons of light to energize electrons that are then transferred through a variety of coenzymes and cofactors to reduce plastoquinone to plastoquinol. The energized electrons are replaced by oxidizing water to form hydrogen ions and molecular oxygen. By replenishing lost electrons with electrons from the splitting of water, photosystem II provides the electrons for all of photosynthesis to occur. The hydrogen ions (protons) generated by the oxidation of water help to create a proton gradient that is used by ATP synthase to generate ATP. The energized electrons transferred to plastoquinone are ultimately used to reduce to NADPH or are used in non-cyclic electron flow. DCMU is a chemical often used in laboratory sett ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
P700
P700, or photosystem I primary donor, is the reaction-center chlorophyll ''a'' molecular dimer associated with photosystem I in plants, algae, and cyanobacteria. Etymology Its name is derived from the word “pigment” (P) and the presence of a major bleaching band centered around 695-700 nm in the flash-induced absorbance difference spectra of P700/ P700+•. Components The structure of P700 consists of a heterodimer with two distinct chlorophyll molecules, most notably chlorophyll ''a'' and chlorophyll ''a''’, giving it an additional name of “special pair”. Inevitably, however, the special pair of P700 behaves as if it were just one unit. This species is vital due to its ability to absorb light energy with a wavelength approximately between 430 nm-700 nm, and transfer high-energy electrons to a series of acceptors that are situated near it. Action and functions Photosystem I operates with the functions of producing NADPH, the reduced form of NADP, at ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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