|
Photosystem Model
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, wh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Complex
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multidomain enzymes, in which multiple active site, catalytic domains are found in a single polypeptide chain. Protein complexes are a form of protein quaternary structure, quaternary structure. Proteins in a protein complex are linked by non-covalent interactions, non-covalent protein–protein interactions. These complexes are a cornerstone of many (if not most) biological processes. The cell is seen to be composed of modular supramolecular complexes, each of which performs an independent, discrete biological function. Through proximity, the speed and selectivity of binding interactions between Enzyme, enzymatic complex and substrates can be vastly improved, leading to higher cellular efficiency. Many of the techniques used to enter cells and isolate proteins are inherently disruptive to such large complexes, complicating the task of determining ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Iron–sulfur Cluster
Iron–sulfur clusters 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. It is supposed that the last universal common ancestor had many iron-sulfur clusters. In biology Iron–sulfur clusters occur in many biological systems, often as components of electron transfer proteins. The ferredoxin proteins are the most common Fe–S proteins in nature. They feature either 2Fe–2S or 4Fe–4S centers. They occur in all branches of life. Fe–S clusters can be classified according to their Fe:S stoichiometry Fe–2S Fe–3S Fe–4S and Fe–4S The Fe–4Sclusters occur in two forms: normal ferredoxins and high potential iron proteins (HiPIP). Both adopt cuboidal structures, but they utilize different oxidation states. They are f ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carotenoids
Carotenoids () are yellow, orange, and red organic compound, organic pigments that are produced by plants and algae, as well as several bacteria, archaea, and Fungus, fungi. Carotenoids give the characteristic color to pumpkins, carrots, parsnips, maize, corn, tomatoes, Domestic Canary, canaries, flamingos, salmon, lobster, shrimp, and daffodils. Over 1,100 identified carotenoids can be further categorized into two classes xanthophylls (which contain oxygen) and carotenes (which are purely hydrocarbons and contain no oxygen). All are derivative (chemistry), derivatives of tetraterpenes, meaning that they are produced from 8 isoprene units and contain 40 carbon atoms. In general, carotenoids absorb wavelengths ranging from 400 to 550 nanometers (violet to green light). This causes the compounds to be deeply colored yellow, orange, or red. Carotenoids are the dominant pigment in autumn leaf coloration of about 15-30% of tree species, but many plant colors, especially reds and purpl ... [...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 benzene.html" ;"title="uch as benzene">uch 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 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 quinaquina in the indigenous languages of Peruvian tribes. Properties Quinones are oxidized derivatives of aromatic compounds an ... [...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 organism, 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-Electron excitation, 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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nanometer
330px, Different lengths as in respect to the Molecule">molecular scale. The nanometre (international spelling as used by the International Bureau of Weights and Measures; SI symbol: nm), or nanometer (American spelling Despite the various list of dialects of English, English dialects spoken from country to country and within different regions of the same country, there are only slight regional variations in English orthography, the two most notable variati ...), is a units of measurement, unit of length in the International System of Units (SI), equal to one billionth (short scale) or one thousand million (long scale) of a metre, meter (0.000000001 m) and to 1000 picometres. One nanometre can be expressed in scientific notation as 1 × 10−9 m and as m. History The nanometre was formerly known as the "''millimicrometre''" – or, more commonly, the "''millimicron''" for short – since it is of a micrometre, micrometer. It was often de ... [...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 hetero dimer 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 Excitat ... [...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 se ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
P700
P700, or photosystem I primary donor, is a molecular dimer of chlorophyll ''a'' associated with the reaction-center of 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, like ''Fe-S complex, Ferridoxyn(FD), which have a higher redox potential i.e. greater affinity to electron' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photosystem 1
Photosystem I (PSI, or plastocyanin–ferredoxin oxidoreductase) is one of two photosystems in the photosynthetic light reactions of algae, plants, and cyanobacteria. Photosystem I is an integral membrane protein complex that uses light energy to catalyze the transfer of electrons across the thylakoid membrane from plastocyanin to ferredoxin. Ultimately, the electrons that are transferred by Photosystem I are used to produce the moderate-energy hydrogen carrier NADPH. The photon energy absorbed by Photosystem I also produces a proton-motive force that is used to generate ATP. PSI is composed of more than 110 cofactors, significantly more than Photosystem II. History This photosystem is known as PSI because it was discovered before Photosystem II, although future experiments showed that Photosystem II is actually the first enzyme of the photosynthetic electron transport chain. Aspects of PSI were discovered in the 1950s, but the significance of these discoveri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
