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Plastocyanin
Plastocyanin is a copper-containing protein that mediates electron-transfer. It is found in a variety of plants, where it participates in photosynthesis. The protein is a prototype of the blue copper proteins, a family of intensely blue-colored metalloproteins. Specifically, it falls into the group of small type I blue copper proteins called "cupredoxins". Function In photosynthesis, plastocyanin functions as an electron transfer agent between cytochrome f of the cytochrome ''b''6''f'' complex from photosystem II and P700+ from photosystem I. Cytochrome ''b''6''f'' complex and P700+ are both membrane-bound proteins with exposed residues on the lumen-side of the thylakoid membrane of chloroplasts. Cytochrome f acts as an electron donor while P700+ accepts electrons from reduced plastocyanin. Structure The copper site in plastocyanin, with the four amino acids that bind the metal labelled. Plastocyanin was the first of the blue copper proteins to be characterised by ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome B6f Complex
The cytochrome ''b''6''f'' complex (plastoquinol/plastocyanin reductase or plastoquinol/plastocyanin oxidoreductase; ) is an enzyme found in the thylakoid membrane in chloroplasts of plants, cyanobacteria, and green algae, that catalyzes the transfer of electrons from plastoquinol to plastocyanin: : plastoquinol + 2 oxidized plastocyanin + 2 H+ ide 1\rightleftharpoons plastoquinone + 2 reduced plastocyanin + 4 H+ ide 2 The reaction is analogous to the reaction catalyzed by cytochrome bc1 (Complex III) of the mitochondrial electron transport chain. During photosynthesis, the cytochrome b6f complex is one step along the chain that transfers electrons from Photosystem II to Photosystem I, and at the same time pumps protons into the thylakoid space, contributing to the generation of an electrochemical (energy) gradient that is later used to synthesize ATP from ADP. Enzyme structure The cytochrome b6f complex is a dimer, with each monomer composed of eight subunits. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Copper Protein
Copper proteins are proteins that contain one or more copper ions as prosthetic groups. Copper proteins are found in all forms of air-breathing life. These proteins are usually associated with electron-transfer with or without the involvement of oxygen (O2). Some organisms even use copper proteins to carry oxygen instead of iron proteins. A prominent copper protein in humans is in cytochrome c oxidase (cco). This enzyme cco mediates the controlled combustion that produces ATP. Other copper proteins include some superoxide dismutases used in defense against free radicals, peptidyl-α-monooxygenase for the production of hormones, and tyrosinase, which affects skin pigmentation. Classes The metal centers in the copper proteins can be classified into several types: * Type I copper centres (T1Cu) are characterized by a single copper atom coordinated by two histidine residues and a cysteine residue in a trigonal planar structure, and a variable axial ligand. In class I T1Cu pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thylakoid
Thylakoids are membrane-bound compartments inside chloroplasts and cyanobacterium, cyanobacteria. They are the site of the light-dependent reactions of photosynthesis. Thylakoids consist of a #Membrane, thylakoid membrane surrounding a #Lumen, thylakoid lumen. Chloroplast thylakoids frequently form stacks of disks referred to as #Granum and stroma lamellae, grana (singular: ''granum''). Grana are connected by intergranal or Stroma (fluid), 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 language, 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 (fluid), stroma. A stack of thy ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photosystem I
Photosystem I (PSI, or plastocyanin–ferredoxin oxidoreductase) is one of two photosystems in the Light-dependent reactions, photosynthetic light reactions of algae, plants, and cyanobacteria. Photosystem I is an integral membrane protein Protein complex, complex that uses light energy to catalyze the electron transfer, 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 Chemiosmosis, proton-motive force that is used to generate adenosine triphosphate, ATP. PSI is composed of more than 110 Cofactor (biochemistry), 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 phot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Metalloprotein
Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins. Abundance It is estimated that approximately half of all proteins contain a metal. In another estimate, about one quarter to one third of all proteins are proposed to require metals to carry out their functions. Thus, metalloproteins have many different functions in cells, such as storage and transport of proteins, enzymes and signal transduction proteins, or infectious diseases. The abundance of metal binding proteins may be inherent to the amino acids that proteins use, as even artificial proteins without evolutionary history will readily bind metals. Most metals in the human body are bound to proteins. For instance, the relatively high concentration of iron in the human body ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Copper
Copper is a chemical element; it has symbol Cu (from Latin ) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. A freshly exposed surface of pure copper has a pinkish-orange color. Copper is used as a conductor of heat and electricity, as a building material, and as a constituent of various metal alloys, such as sterling silver used in jewelry, cupronickel used to make marine hardware and coins, and constantan used in strain gauges and thermocouples for temperature measurement. Copper is one of the few metals that can occur in nature in a directly usable, unalloyed metallic form. This means that copper is a native metal. This led to very early human use in several regions, from . Thousands of years later, it was the first metal to be smelted from sulfide ores, ; the first metal to be cast into a shape in a mold, ; and the first metal to be purposely alloyed with another metal, tin, to create bronze, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photosynthesis
Photosynthesis ( ) is a system of biological processes by which photosynthetic organisms, such as most plants, algae, and cyanobacteria, convert light energy, typically from sunlight, into the chemical energy necessary to fuel their metabolism. ''Photosynthesis'' usually refers to oxygenic photosynthesis, a process that produces oxygen. Photosynthetic organisms store the chemical energy so produced within intracellular organic compounds (compounds containing carbon) like sugars, glycogen, cellulose and starches. To use this stored chemical energy, an organism's cells metabolize the organic compounds through cellular respiration. Photosynthesis plays a critical role in producing and maintaining the oxygen content of the Earth's atmosphere, and it supplies most of the biological energy necessary for complex life on Earth. Some bacteria also perform anoxygenic photosynthesis, which uses bacteriochlorophyll to split hydrogen sulfide as a reductant instead of water, p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome F
Cytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are involved in the electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d. Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core. In addition to the classification by the IUBMB into four cytochrome classes, several additional classifications such as cytochrome o and cytochrome P450 can be found in biochemical literature. History Cytochromes were initially described in 1884 by Charles Alexander MacMunn as respiratory pigments (myohematin or histohematin). In the 1920s, Keilin rediscovered these respiratory pigments and n ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cysteine
Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the chemical formula, formula . The thiol side chain in cysteine enables the formation of Disulfide, disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. LCysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Ancient Greek, Greek κύστις ''kýstis'', "bladder". The thiol is susceptible to oxidation to give the disulfide bond, disulfide derivative cystine, which serves an important structural role in many proteins. In this case, the symbol Cyx is sometimes used. The deprotonated form can generally be described by the symbol Cym as well. When used as a food additive, cysteine has the E number E920. Cysteine is Genetic code, encoded by the codo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron-transfer
Electron transfer (ET) occurs when an electron relocates from an atom, ion, or molecule, to another such chemical entity. ET describes the mechanism by which electrons are transferred in redox reactions. Electrochemical processes are ET reactions. ET reactions are relevant to photosynthesis and respiration and commonly involve transition metal complexes. In organic chemistry ET is a step in some industrial polymerization reactions. It is foundational to photoredox catalysis. Classes of electron transfer Inner-sphere electron transfer In inner-sphere ET, two redox centers are covalently linked during the ET. This bridge can be permanent, in which case the electron transfer event is termed intramolecular electron transfer. More commonly, however, the covalent linkage is transitory, forming just prior to the ET and then disconnecting following the ET event. In such cases, the electron transfer is termed intermolecular electron transfer. A famous example of an inner sphere ET proces ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phormidium
''Phormidium'' is a genus of cyanobacteria in the family Oscillatoriaceae. As a result of recent genetic analyses, several new genera were erected from this genus, e.g. '' Potamolinea''. Species 83, including * '' Phormidium ambiguum'' * '' Phormidium allorgei'' * ''Phormidium aerugineo-caeruleum'' * '' Phormidium lucidum'' * '' Phormidium subfuscum'' Moved: * ''Phormidium africanum'' → '' Leptolyngbya africana'' * ''Phormidium formosum'' → '' Kamptonema formosum''LPSN List of Prokaryotic names with Standing in Nomenclature (LPSN) is an online database that maintains information on the naming and taxonomy image:Hierarchical clustering diagram.png, 280px, Generalized scheme of taxonomy Taxonomy is a practi ...Species ''Phormidium formosum'' References Cyanobacteria genera {{Cyanobacteria-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
