A copper-containing plant protein that is a fundamental link in the electron transport chain of green plants during the photosynthetic conversion of light energy by photophosphorylation into the potential energy of chemical bonds.
Cytochromes f are found as components of the CYTOCHROME B6F COMPLEX. They play important role in the transfer of electrons from PHOTOSYSTEM I to PHOTOSYSTEM II.
Cytochromes of the c type that are involved in the transfer of electrons from CYTOCHROME B6F COMPLEX and PHOTOSYSTEM I.
A large multisubunit protein complex that is found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to drive electron transfer reactions that result in either the reduction of NADP to NADPH or the transport of PROTONS across the membrane.
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
A form-genus of CYANOBACTERIA in the order Nostocales. Trichomes composed of spherical or ovoid vegetative cells along with heterocysts and akinetes. The species form symbiotic associations with a wide range of eukaryotes.
A genus of PROCHLOROPHYTES occurring in unbranched chains of indefinite length and containing both chlorophylls a and b.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
A phylum of photosynthetic EUKARYOTA bearing double membrane-bound plastids containing chlorophyll a and b. They comprise the classical green algae, and represent over 7000 species that live in a variety of primarily aquatic habitats. Only about ten percent are marine species, most live in freshwater.
A protein complex that includes CYTOCHROME B6 and CYTOCHROME F. It is found in the THYLAKOID MEMBRANE and plays an important role in process of PHOTOSYNTHESIS by transferring electrons from PLASTOQUINONE to PLASTOCYANIN or CYTOCHROME C6. The transfer of electrons is coupled to the transport of PROTONS across the membrane.
A bacterial protein from Pseudomonas, Bordetella, or Alcaligenes which operates as an electron transfer unit associated with the cytochrome chain. The protein has a molecular weight of approximately 16,000, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308nm.
Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.
A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE.
Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Carbodiimide cross-linking reagent.
A species of GREEN ALGAE. Delicate, hairlike appendages arise from the flagellar surface in these organisms.
The accumulation of an electric charge on a object
A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)
A genus of CYANOBACTERIA consisting of trichomes that are untapered with conspicuous constrictions at cross-walls. A firm individual sheath is absent, but a soft covering is often present. Many species are known worldwide as major components of freshwater PLANKTON and also of many saline lakes. The species ANABAENA FLOS-AQUAE is responsible for acute poisonings of various animals.
Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX.

Balanced regulation of expression of the gene for cytochrome cM and that of genes for plastocyanin and cytochrome c6 in Synechocystis. (1/252)

The cytM gene for cytochrome cM was previously found in Synechocystis sp. PCC 6803. Northern blotting analysis revealed that the cytM gene was scarcely expressed under normal growth conditions but its expression was enhanced when cells were exposed to low temperature or high-intensity light. By contrast, the expression of the genes for cytochrome c6 and plastocyanin was suppressed at low temperature or under high-intensity light. These observations suggest that plastocyanin and/or cytochrome c6, which are dominant under non-stressed conditions, are replaced by cytochrome cM under the stress conditions.  (+info)

The structure and unusual pH dependence of plastocyanin from the fern Dryopteris crassirhizoma. The protonation of an active site histidine is hindered by pi-pi interactions. (2/252)

Spectroscopic properties, amino acid sequence, electron transfer kinetics, and crystal structures of the oxidized (at 1.7 A resolution) and reduced form (at 1.8 A resolution) of a novel plastocyanin from the fern Dryopteris crassirhizoma are presented. Kinetic studies show that the reduced form of Dryopteris plastocyanin remains redox-active at low pH, under conditions where the oxidation of the reduced form of other plastocyanins is inhibited by the protonation of a solvent-exposed active site residue, His87 (equivalent to His90 in Dryopteris plastocyanin). The x-ray crystal structure analysis of Dryopteris plastocyanin reveals pi-pi stacking between Phe12 and His90, suggesting that the active site is uniquely protected against inactivation. Like higher plant plastocyanins, Dryopteris plastocyanin has an acidic patch, but this patch is located closer to the solvent-exposed active site His residue, and the total number of acidic residues is smaller. In the reactions of Dryopteris plastocyanin with inorganic redox reagents, the acidic patch (the "remote" site) and the hydrophobic patch surrounding His90 (the "adjacent" site) are equally efficient for electron transfer. These results indicate the significance of the lack of protonation at the active site of Dryopteris plastocyanin, the equivalence of the two electron transfer sites in this protein, and a possibility of obtaining a novel insight into the photosynthetic electron transfer system of the first vascular plant fern, including its molecular evolutionary aspects. This is the first report on the characterization of plastocyanin and the first three-dimensional protein structure from fern plant.  (+info)

Crystal structures of wild-type and mutant plastocyanins from a higher plant, Silene. (3/252)

Plastocyanin functions as an electron carrier between the cytochrome b6f complex and photosystem I. The crystal structures of the wild-type and E43K/D44K double mutant from the higher plant, Silene, have been determined at 2.0 and 1.75 A resolution, respectively. The wild-type plastocyanin comprises two monomers per asymmetric unit, one of which shows the unusually great distance between the copper ion and the Ndelta1 atom of H87 because of the hydrogen bond network formation between H87 and symmetry-related G10. The root mean square deviation for Ca atoms between the wild-type and mutant plastocyanins is 0.44 A, however, the electrostatic potential maps of their molecular surfaces are remarkably different. The low electron-transfer rate in the E43K/D44K mutant results from the hindrance of electrostatic interactions, not from the structural change due to the mutation.  (+info)

Site-directed mutagenesis of cytochrome c6 from Synechocystis sp. PCC 6803. The heme protein possesses a negatively charged area that may be isofunctional with the acidic patch of plastocyanin. (4/252)

This paper reports the first site-directed mutagenesis analysis of any cytochrome c6, a heme protein that performs the same function as the copper-protein plastocyanin in the electron transport chain of photosynthetic organisms. Photosystem I reduction by the mutants of cytochrome c6 from the cyanobacterium Synechocystis sp. PCC 6803 has been studied by laser flash absorption spectroscopy. Their kinetic efficiency and thermodynamic properties have been compared with those of plastocyanin mutants from the same organism. Such a comparative study reveals that aspartates at positions 70 and 72 in cytochrome c6 are located in an acidic patch that may be isofunctional with the well known "south-east" patch of plastocyanin. Calculations of surface electrostatic potential distribution in the mutants of cytochrome c6 and plastocyanin indicate that the changes in protein reactivity depend on the surface electrostatic potential pattern rather than on the net charge modification induced by mutagenesis. Phe-64, which is close to the heme group and may be the counterpart of Tyr-83 in plastocyanin, does not appear to be involved in the electron transfer to photosystem I. In contrast, Arg-67, which is at the edge of the cytochrome c6 acidic area, seems to be crucial for the interaction with the reaction center.  (+info)

Lipid composition determines the effects of arbutin on the stability of membranes. (5/252)

Arbutin (hydroquinone-beta-D-glucopyranoside) is an abundant solute in the leaves of many freezing- or desiccation-tolerant plants. Its physiological role in plants, however, is not known. Here we show that arbutin protects isolated spinach (Spinacia oleracea L.) thylakoid membranes from freeze-thaw damage. During freezing of liposomes, the presence of only 20 mM arbutin led to complete leakage of a soluble marker from egg PC (EPC) liposomes. When the nonbilayer-forming chloroplast lipid monogalactosyldiacylglycerol (MGDG) was included in the membranes, this leakage was prevented. Inclusion of more than 15% MGDG into the membranes led to a strong destabilization of liposomes during freezing. Under these conditions arbutin became a cryoprotectant, as only 5 mM arbutin reduced leakage from 75% to 20%. The nonbilayer lipid egg phosphatidylethanolamine (EPE) had an effect similar to that of MGDG, but was much less effective, even at concentrations up to 80% in EPC membranes. Arbutin-induced leakage during freezing was accompanied by massive bilayer fusion in EPC and EPC/EPE membranes. Twenty percent MGDG in EPC bilayers completely inhibited the fusogenic effect of arbutin. The membrane surface probes merocyanine 540 and 2-(6-(7-nitrobenz-2-oxa-1, 3-diazol-4-yl)amino)hexanoyl-1-hexadecanoyl-sn-glycero-3-phosph ocholi ne (NBD-C(6)-HPC) revealed that arbutin reduced the ability of both probes to partition into the membranes. Steady-state anisotropy measurements with probes that localize at different positions in the membranes showed that headgroup mobility was increased in the presence of arbutin, whereas the mobility of the fatty acyl chains close to the glycerol backbone was reduced. This reduction, however, was not seen in membranes containing 20% MGDG. The effect of arbutin on lipid order was limited to the interfacial region of the membranes and was not evident in the hydrophobic core region. From these data we were able to derive a physical model of the perturbing or nonperturbing interactions of arbutin with lipid bilayers.  (+info)

Accumulation of pre-apocytochrome f in a Synechocystis sp. PCC 6803 mutant impaired in cytochrome c maturation. (6/252)

Cytochrome c maturation involves heme transport and covalent attachment of heme to the apoprotein. The 5' end of the ccsB gene, which is involved in the maturation process and resembles the ccs1 gene from Chlamydomonas reinhardtii, was replaced by a chloramphenicol resistance cartridge in the cyanobacterium Synechocystis sp. PCC 6803. The resulting Delta(M1-A24) mutant lacking the first 24 ccsB codons grew only under anaerobic conditions. The mutant retained about 20% of the wild-type amount of processed cytochrome f with heme attached, apparently assembled in a functional cytochrome b(6)f complex. Moreover, the mutant accumulated unprocessed apocytochrome f in its membrane fraction. A pseudorevertant was isolated that regained the ability to grow under aerobic conditions. The locus of the second-site mutation was mapped to ccsB, and the mutation resulted in the formation of a new potential start codon in the intergenic region, between the chloramphenicol resistance marker and ccsB, in frame with the remaining part of ccsB. In this pseudorevertant the amount of holocyt f increased, whereas that of unprocessed apocytochrome f decreased. We suggest that the original deletion mutant Delta(M1-A24) expresses an N-terminally truncated version of the protein. The stable accumulation of unprocessed apocytochrome f in membranes of the Delta(M1-A24) mutant may be explained by its association with truncated and only partially functional CcsB protein resulting in protection from degradation. Our attempt to delete the first 244 codons of ccsB in Synechocystis sp. PCC 6803 was not successful, suggesting that this would lead to a lack of functional cytochrome b(6)f complex. The results suggest that the CcsB protein is an apocytochrome chaperone, which together with CcsA may constitute part of cytochrome c lyase.  (+info)

Electron transfers amongst cytochrome f, plastocyanin and photosystem I: kinetics and mechanisms. (7/252)

The review covers the theory and practice of the determination of kinetic constants for the electron transfer reactions in chloroplast thylakoid membranes between plastocyanin and cytochrome f in cytochrome bf complexes, and between plastocyanin and the reaction centre of photosystem I. Effects of ionic strength and pH are featured. The contribution of mutant studies is included. It is concluded that nearly all data from in vitro experiments can be interpreted with a reaction scheme in which an encounter complex between donor and acceptor is formed by long-range electrostatic attraction, followed by rearrangement during which metal centres become close enough for rapid intra-complex electron transfer. In vivo experiments so far cast doubt on this particular sequence, but their interpretation is not straightforward. Means of modelling the bimolecular complex between cytochrome f and plastocyanin are outlined, and two likely structures are illustrated. The complex formed by plastocyanin and photosystem I in higher plants involves the PsaF subunit, but its structure has not been fully determined.  (+info)

Redox- and pH-dependent association of plastocyanin with lipid bilayers: effect on protein conformation and thermal stability. (8/252)

The effect of electrostatic interactions on the conformation and thermal stability of plastocyanin (Pc) was studied by infrared spectroscopy. Association of any of the two redox states of the protein with positively charged membranes at neutral pH does not significantly change the secondary structure of Pc. However, upon membrane binding, the denaturation temperature decreases, regardless of the protein redox state. The extent of destabilization depends on the proportion of positively charged lipid headgroups in the membrane, becoming greater as the surface density of basic phospholipids increases. In contrast, at pH 4.8 the membrane binding-dependent conformational change becomes redox-sensitive. While the secondary structures and thermal stabilities of free and membrane-bound oxidized Pc are similar under acidic conditions, the conformation of the reduced form of the protein drastically rearranges upon membrane association. This rearrangement does not depend on electrostatic interactions to occur, since it is also observed in the presence of uncharged lipid bilayers. The conformational transition, only observed for reduced Pc, involves the exposure of hydrophobic regions that leads to intermolecular interactions at the membrane surface. Membrane-mediated partial unfolding of reduced Pc can be reversed by readjusting the pH to neutrality, in the absence of electrostatic interactions. This redox-dependent behavior might reflect specific structural requirements for the interaction of Pc with its redox partners.  (+info)

Plastocyanin is a small, copper-containing protein that plays a crucial role in the photosynthetic electron transport chain. It functions as an electron carrier, facilitating the movement of electrons between two key protein complexes (cytochrome b6f and photosystem I) located in the thylakoid membrane of chloroplasts. Plastocyanin is a soluble protein found in the lumen of the thylakoids, and its copper ion serves as the site for electron transfer. The oxidized form of plastocyanin accepts an electron from cytochrome b6f and then donates it to photosystem I, helping to maintain the flow of electrons during light-dependent reactions in photosynthesis.

Cytochrome f is a type of cytochrome protein that contains heme as a cofactor and plays a role in the electron transport chain during photosynthesis. It is specifically located in the cytochrome b6f complex, which is found in the thylakoid membrane of chloroplasts in plants and algae.

Cytochrome f functions as a ubiquinol-plastoquinone oxidoreductase, accepting electrons from ubiquinol and transferring them to plastoquinone. This electron transfer process is an essential step in the generation of a proton gradient across the thylakoid membrane, which drives the synthesis of ATP during photosynthesis.

Deficiency or mutation in cytochrome f can lead to impaired photosynthetic efficiency and reduced growth in plants.

Cytochrome c6 is a type of cytochrome protein that contains heme as a cofactor and functions as an electron transporter in the electron transport chain during photosynthesis. It is found primarily in certain bacteria, algae, and some lower eukaryotes. The "c6" designation refers to its molecular weight and structure, which is similar to that of cytochrome c found in mitochondria. However, cytochrome c6 has a higher redox potential than cytochrome c and plays a role in the water-splitting reaction during photosynthesis. It is involved in the transfer of electrons from the cytochrome b6f complex to the photosystem I.

Photosystem I Protein Complex, also known as PsaA/B-Protein or Photosystem I reaction center, is a large protein complex found in the thylakoid membrane of plant chloroplasts and cyanobacteria. It plays a crucial role in light-dependent reactions of photosynthesis, where it absorbs light energy and converts it into chemical energy in the form of NADPH.

The complex is composed of several subunits, including PsaA and PsaB, which are the core components that bind to chlorophyll a and bacteriochlorophyll a pigments. These pigments absorb light energy and transfer it to the reaction center, where it is used to drive the electron transport chain and generate a proton gradient across the membrane. This gradient is then used to produce ATP, which provides energy for the carbon fixation reactions in photosynthesis.

Photosystem I Protein Complex is also involved in cyclic electron flow, where electrons are recycled within the complex to generate additional ATP without producing NADPH. This process helps regulate the balance between ATP and NADPH production in the chloroplast and optimizes the efficiency of photosynthesis.

Cytochromes are a type of hemeprotein found in the mitochondria and other cellular membranes of organisms. They contain a heme group, which is a prosthetic group composed of an iron atom surrounded by a porphyrin ring. This structure allows cytochromes to participate in redox reactions, acting as electron carriers in various biological processes.

There are several types of cytochromes, classified based on the type of heme they contain and their absorption spectra. Some of the most well-known cytochromes include:

* Cytochrome c: a small, mobile protein found in the inner mitochondrial membrane that plays a crucial role in the electron transport chain during cellular respiration.
* Cytochrome P450: a large family of enzymes involved in the metabolism of drugs, toxins, and other xenobiotics. They are found in various tissues, including the liver, lungs, and skin.
* Cytochrome b: a component of several electron transport chains, including those found in mitochondria, bacteria, and chloroplasts.

Cytochromes play essential roles in energy production, detoxification, and other metabolic processes, making them vital for the survival and function of living organisms.

"Spinacia oleracea" is the scientific name for a plant species, not a medical term. It is commonly known as spinach, a leafy green vegetable. While spinach has many health benefits and is often recommended as part of a balanced diet, it does not have a specific medical definition.

Spinach is rich in various nutrients such as iron, calcium, vitamin A, vitamin C, and folic acid. It can contribute to overall health, support immune function, and provide antioxidant benefits. However, it is important to note that 'Spinacia oleracea' itself does not have a medical definition.

Nostoc is not a medical term, but a genus of cyanobacteria (blue-green algae) that can form colonies in various aquatic and terrestrial environments. Some species of nostoc are capable of forming gelatinous masses or "mats" that can be found in freshwater bodies, soils, and even on the surface of rocks and stones.

While nostoc itself is not a medical term, it has been studied in the context of medicine due to its potential health benefits. Some research suggests that nostoc may have anti-inflammatory, antioxidant, and antimicrobial properties, among others. However, more studies are needed to fully understand the potential therapeutic uses of nostoc and its safety for human consumption or use in medical treatments.

I'm sorry for any confusion, but "Prochlorothrix" doesn't have a widely accepted medical definition. It is a genus name in the family of Cyanobacteria, which are bacteria that can photosynthesize like plants. They are sometimes referred to as blue-green algae. Prochlorothrix species have been found in various environments such as freshwater, soil, and lichens. They are not typically associated with human diseases or medical conditions. If you have any specific concerns or questions related to this term, I would recommend consulting a healthcare professional or a microbiologist for more accurate and contextual information.

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration. It is the final pathway for electrons derived from the oxidation of nutrients such as glucose, fatty acids, and amino acids to be transferred to molecular oxygen. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to produce ATP, the main energy currency of the cell.

The electron transport chain consists of four complexes (I-IV) and two mobile electron carriers (ubiquinone and cytochrome c). Electrons from NADH and FADH2 are transferred to Complex I and Complex II respectively, which then pass them along to ubiquinone. Ubiquinone then transfers the electrons to Complex III, which passes them on to cytochrome c. Finally, cytochrome c transfers the electrons to Complex IV, where they combine with oxygen and protons to form water.

The transfer of electrons through the ETC is accompanied by the pumping of protons from the mitochondrial matrix to the intermembrane space, creating a proton gradient. The flow of protons back across the inner membrane through ATP synthase drives the synthesis of ATP from ADP and inorganic phosphate.

Overall, the electron transport chain is a crucial process for generating energy in the form of ATP in the cell, and it plays a key role in many metabolic pathways.

Copper is a chemical element with the symbol Cu (from Latin: *cuprum*) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. Copper is found as a free element in nature, and it is also a constituent of many minerals such as chalcopyrite and bornite.

In the human body, copper is an essential trace element that plays a role in various physiological processes, including iron metabolism, energy production, antioxidant defense, and connective tissue synthesis. Copper is found in a variety of foods, such as shellfish, nuts, seeds, whole grains, and organ meats. The recommended daily intake of copper for adults is 900 micrograms (mcg) per day.

Copper deficiency can lead to anemia, neutropenia, impaired immune function, and abnormal bone development. Copper toxicity, on the other hand, can cause nausea, vomiting, abdominal pain, diarrhea, and in severe cases, liver damage and neurological symptoms. Therefore, it is important to maintain a balanced copper intake through diet and supplements if necessary.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

Photosynthetic Reaction Center (RC) Complex Proteins are specialized protein-pigment structures that play a crucial role in the primary process of light-driven electron transport during photosynthesis. They are present in the thylakoid membranes of cyanobacteria, algae, and higher plants.

The Photosynthetic Reaction Center Complex Proteins are composed of two major components: the light-harvesting complex (LHC) and the reaction center (RC). The LHC contains antenna pigments like chlorophylls and carotenoids that absorb sunlight and transfer the excitation energy to the RC. The RC is a multi-subunit protein complex containing cofactors such as bacteriochlorophyll, pheophytin, quinones, and iron-sulfur clusters.

When a photon of light is absorbed by the antenna pigments in the LHC, the energy is transferred to the RC, where it initiates a charge separation event. This results in the transfer of an electron from a donor molecule to an acceptor molecule, creating a flow of electrical charge and generating a transmembrane electrochemical gradient. The energy stored in this gradient is then used to synthesize ATP and reduce NADP+, which are essential for carbon fixation and other metabolic processes in the cell.

In summary, Photosynthetic Reaction Center Complex Proteins are specialized protein structures involved in capturing light energy and converting it into chemical energy during photosynthesis, ultimately driving the synthesis of ATP and NADPH for use in carbon fixation and other metabolic processes.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

Chlorophyta is a division of green algae, also known as green plants. This group includes a wide variety of simple, aquatic organisms that contain chlorophylls a and b, which gives them their characteristic green color. They are a diverse group, ranging from unicellular forms to complex multicellular seaweeds. Chlorophyta is a large and varied division with approximately 7,00

The cytochrome b6f complex is a protein complex in the thylakoid membrane of the chloroplasts in plants, algae, and cyanobacteria. It plays a crucial role in the light-dependent reactions of photosynthesis by facilitating the transfer of electrons from photosystem II to photosystem I.

The complex is composed of four subunits: cytochrome b6, subunit IV, and two Rieske iron-sulfur proteins. Cytochrome b6 is a heme protein that contains two heme groups, while subunit IV helps anchor the complex in the thylakoid membrane. The Rieske iron-sulfur proteins contain a 2Fe-2S cluster and are responsible for transferring electrons between cytochrome b6 and plastoquinone, a mobile electron carrier.

The cytochrome b6f complex functions in the Q-cycle, which is a mechanism that increases the efficiency of electron transfer and generates a proton gradient across the thylakoid membrane. This proton gradient drives the synthesis of ATP, an essential energy currency for the cell. Overall, the cytochrome b6f complex is a vital component of the photosynthetic machinery, enabling the conversion of light energy into chemical energy in the form of ATP and NADPH.

Azurin is a small protein with a blue copper center, which is involved in electron transfer reactions. It is produced by the bacterium *Pseudomonas aeruginosa*, and has been studied for its potential role in wound healing and as an anticancer agent. The name "azurin" comes from the fact that this protein has a bright blue color due to its copper ion content.

Chloroplasts are specialized organelles found in the cells of green plants, algae, and some protists. They are responsible for carrying out photosynthesis, which is the process by which these organisms convert light energy from the sun into chemical energy in the form of organic compounds, such as glucose.

Chloroplasts contain the pigment chlorophyll, which absorbs light energy from the sun. They also contain a system of membranes and enzymes that convert carbon dioxide and water into glucose and oxygen through a series of chemical reactions known as the Calvin cycle. This process not only provides energy for the organism but also releases oxygen as a byproduct, which is essential for the survival of most life forms on Earth.

Chloroplasts are believed to have originated from ancient cyanobacteria that were engulfed by early eukaryotic cells and eventually became integrated into their host's cellular machinery through a process called endosymbiosis. Over time, chloroplasts evolved to become an essential component of plant and algal cells, contributing to their ability to carry out photosynthesis and thrive in a wide range of environments.

Cyanobacteria, also known as blue-green algae, are a type of bacteria that obtain their energy through photosynthesis, similar to plants. They can produce oxygen and contain chlorophyll a, which gives them a greenish color. Some species of cyanobacteria can produce toxins that can be harmful to humans and animals if ingested or inhaled. They are found in various aquatic environments such as freshwater lakes, ponds, and oceans, as well as in damp soil and on rocks. Cyanobacteria are important contributors to the Earth's oxygen-rich atmosphere and play a significant role in the global carbon cycle.

Chlorophyll is a green pigment found in the chloroplasts of photosynthetic plants, algae, and some bacteria. It plays an essential role in light-dependent reactions of photosynthesis by absorbing light energy, primarily from the blue and red parts of the electromagnetic spectrum, and converting it into chemical energy to fuel the synthesis of carbohydrates from carbon dioxide and water. The structure of chlorophyll includes a porphyrin ring, which binds a central magnesium ion, and a long phytol tail. There are several types of chlorophyll, including chlorophyll a and chlorophyll b, which have distinct absorption spectra and slightly different structures. Chlorophyll is crucial for the process of photosynthesis, enabling the conversion of sunlight into chemical energy and the release of oxygen as a byproduct.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Ethyldimethylaminopropyl carbodiimide (EDC) is a type of chemical compound known as a carbodiimide, which is commonly used in the field of biochemistry and molecular biology as a cross-linking agent. EDC can react with carboxylic acid groups to form an active ester intermediate, which can then react with amino groups to form an amide bond. This property makes it useful for conjugating proteins, peptides, and other molecules that contain carboxyl and amino groups.

The medical definition of EDC is not well established since it is primarily used in research settings rather than in clinical practice. However, it is important to note that EDC can be toxic at high concentrations and should be handled with care. It may also cause irritation to the skin, eyes, and respiratory tract, so appropriate safety precautions should be taken when working with this compound.

Chlamydomonas reinhardtii is a species of single-celled, freshwater green algae. It is commonly used as a model organism in scientific research due to its simple unicellular structure and the ease with which it can be genetically manipulated. C. reinhardtii has a single, large chloroplast that contains both photosynthetic pigments and a nucleomorph, a remnant of a secondary endosymbiotic event where another alga was engulfed by an ancestral eukaryote. This species is capable of both phototactic and photophobic responses, allowing it to move towards or away from light sources. Additionally, C. reinhardtii has two flagella for locomotion, making it a popular subject for ciliary and flagellar research. It undergoes closed mitosis within its single, diploid nucleus, which is surrounded by a cell wall composed of glycoproteins. The genome of C. reinhardtii has been fully sequenced, providing valuable insights into the molecular mechanisms underlying photosynthesis, flagellar assembly, and other fundamental biological processes.

I'm sorry for any confusion, but static electricity is not a term that has a specific medical definition. Static electricity is an electrical charge that builds up on the surface of objects. This occurs when there is an imbalance of electric charges within or on the surface of a material. It can be caused by certain conditions, such as friction, which can build up an electric charge.

While not a medical term, static electricity can have various effects in different settings, including medical ones. For instance, it can cause issues with electronic equipment used in healthcare settings. Additionally, some people may experience a shock or spark when they touch a conductive object that has been charged with static electricity. However, these occurrences are not typically considered medical conditions or issues.

Cytochrome c is a small protein that is involved in the electron transport chain, a key part of cellular respiration in which cells generate energy in the form of ATP. Cytochrome c contains a heme group, which binds to and transports electrons. The cytochrome c group refers to a class of related cytochromes that have similar structures and functions. These proteins are found in the mitochondria of eukaryotic cells (such as those of plants and animals) and in the inner membranes of bacteria. They play a crucial role in the production of energy within the cell, and are also involved in certain types of programmed cell death (apoptosis).

Photosynthesis is not strictly a medical term, but it is a fundamental biological process with significant implications for medicine, particularly in understanding energy production in cells and the role of oxygen in sustaining life. Here's a general biological definition:

Photosynthesis is a process by which plants, algae, and some bacteria convert light energy, usually from the sun, into chemical energy in the form of organic compounds, such as glucose (or sugar), using water and carbon dioxide. This process primarily takes place in the chloroplasts of plant cells, specifically in structures called thylakoids. The overall reaction can be summarized as:

6 CO2 + 6 H2O + light energy → C6H12O6 + 6 O2

In this equation, carbon dioxide (CO2) and water (H2O) are the reactants, while glucose (C6H12O6) and oxygen (O2) are the products. Photosynthesis has two main stages: the light-dependent reactions and the light-independent reactions (Calvin cycle). The light-dependent reactions occur in the thylakoid membrane and involve the conversion of light energy into ATP and NADPH, which are used to power the Calvin cycle. The Calvin cycle takes place in the stroma of chloroplasts and involves the synthesis of glucose from CO2 and water using the ATP and NADPH generated during the light-dependent reactions.

Understanding photosynthesis is crucial for understanding various biological processes, including cellular respiration, plant metabolism, and the global carbon cycle. Additionally, research into artificial photosynthesis has potential applications in renewable energy production and environmental remediation.

Anabaena is a genus of cyanobacteria, also known as blue-green algae. These bacteria are capable of photosynthesis and can form colonies that resemble fine filaments or hair-like structures. Some species of Anabaena are able to fix nitrogen from the atmosphere, making them important contributors to the nitrogen cycle in aquatic ecosystems. In some cases, certain species of Anabaena can produce toxins that can be harmful to other organisms, including humans and animals.

It's worth noting that while Anabaena is a widely used and well-established genus name, recent research has suggested that the traditional classification system for cyanobacteria may not accurately reflect their evolutionary relationships. As a result, some scientists have proposed alternative classification schemes that may lead to changes in the way these organisms are named and classified in the future.

Light-harvesting protein complexes are specialized structures in photosynthetic organisms, such as plants, algae, and some bacteria, that capture and transfer light energy to the reaction centers where the initial chemical reactions of photosynthesis occur. These complexes consist of proteins and pigments (primarily chlorophylls and carotenoids) arranged in a way that allows them to absorb light most efficiently. The absorbed light energy is then converted into electrical charges, which are transferred to the reaction centers for further chemical reactions leading to the production of organic compounds and oxygen. The light-harvesting protein complexes play a crucial role in initiating the process of photosynthesis and optimizing its efficiency by capturing and distributing light energy.

Cytochrome f acts as an electron donor while P700+ accepts electrons from reduced plastocyanin. Plastocyanin was the first of ... Plastocyanin (Cu2+Pc) is reduced (an electron is added) by cytochrome f according to the following reaction: Cu2+Pc + e− → Cu+ ... Plastocyanin performs electron transfer with the redox between Cu(I) and Cu(II), and it was first theorized that its entatic ... Plastocyanin is a copper-containing protein that mediates electron-transfer. It is found in a variety of plants, where it ...
Plastocyanin/azurin family of copper-binding proteins (or blue (type 1) copper domain) is a family of small proteins that bind ... restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 A resolution". Acta Crystallogr. B. 48 (6 ...
Plastocyanin". Journal of Molecular Biology. 226 (3): 819-35. doi:10.1016/0022-2836(92)90634-V. PMID 1507228. Fersht AR ( ...
The electron transport protein plastocyanin is present in the lumen and shuttles electrons from the cytochrome b6f protein ... These carriers are plastoquinone and plastocyanin. Plastoquinone shuttles electrons from photosystem II to the cytochrome b6f ... plastocyanin moves through the thylakoid lumen. The lumen of the thylakoids is also the site of water oxidation by the oxygen ... it is situated between the two photosystems and transfers electrons from photosystem II-plastoquinone to plastocyanin- ...
... plastocyanin, and azurin. Electronic structure of the blue copper sites". Journal of the American Chemical Society. 102 (1): ...
... and plastocyanin (Pc): Cytochrome b6f catalyzes the transfer of electrons from plastoquinol to plastocyanin, while pumping two ... The cytochrome b6f complex (plastoquinol-plastocyanin reductase; EC 1.10.99.1) is an enzyme found in the thylakoid membrane in ... The electron from ferredoxin (Fd) is transferred to plastoquinone and then the cytochrome b6f complex to reduce plastocyanin, ... that catalyzes the transfer of electrons from plastoquinol to plastocyanin. The reaction is analogous to the reaction catalyzed ...
They are then returned (via plastocyanin) to P700. NADPH and ATP are used to synthesize organic molecules from CO 2. The ratio ... Cytochrome b6f transfers the electron chain to PSI through plastocyanin molecules. PSI can continue the electron transfer in ... The mobile water-soluble electron carrier is cytochrome c6 in cyanobacteria, having been replaced by plastocyanin in plants. ... PSII and PSI are connected by a transmembrane proton pump, cytochrome b6f complex (plastoquinol-plastocyanin reductase; EC 1.10 ...
... + recovers its lost electron by oxidizing plastocyanin, which regenerates P700. P680 Photosystem I Photosystem II Chitnis, ... 2006). Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase. Advances in Photosynthesis and Respiration. Vol ... 2006). Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase. Advances in Photosynthesis and Respiration. Vol ... 2006). Photosystem I: The Light-Driven Plastocyanin:Ferredoxin Oxidoreductase. Advances in Photosynthesis and Respiration. Vol ...
... and particularly the electron transport protein plastocyanin. The intensely blue colour of plastocyanin and its unusual redox ... It was not until 1977 that his group finally determined the structure of plastocyanin crystallised from the poplar tree (see ... Working as a crystallographer, Freeman's major legacies are the understanding of plastocyanin and other blue copper proteins, ... Plastocyanin". J. Mol. Biol. 110 (1): 187-189. doi:10.1016/S0022-2836(77)80106-X. PMID 845945. Colman, P. M.; Freeman, H. C.; ...
In an effort to understand copper sensing, she studied mutants that did not produce plastocyanin. She discovered that the ... crystal structure of plastocyanin from the green alga Chlamydomonas reinhardtii". Biochemistry. 32 (40): 10560-10567. doi: ... Merchant was the first to demonstrate that the RNA for Chlamydomonas reinhardtii plastocyanin is produced when copper is ... She used pulse-chase analysis to show that whilst plastocyanin is continuously translated, it becomes degraded in systems ...
Bauerle, C.; Keegstra, K. (1991). "Full-length plastocyanin precursor is translocated across isolated thylakoid membranes". The ... with an early focus on the transport of thylakoid proteins and translocation of plastocyanin precursors in chloroplasts. Some ...
Gideon DA, Nirusimhan V, Manoj KM (March 2022). "Are plastocyanin and ferredoxin specific electron carriers or generic redox ...
Plastocyanin is one of the family of blue copper proteins that are involved in electron transfer reactions. The copper-binding ... In the reduced form of plastocyanin, His-87 will become protonated with a pKa of 4.4. Protonation prevents it acting as a ... "X-Ray Crystal-Structure Analysis of Plastocyanin at 2.7 Å Resolution". Nature. 272 (5651): 319-324. Bibcode:1978Natur.272..319C ...
Plastocyanin is an electron carrier that transfers the electron from cytochrome b6f to the P700 cofactor of PSI in its ionized ... Photosystem I (PSI, or plastocyanin-ferredoxin oxidoreductase) is one of two photosystems in the photosynthetic light reactions ... doi:10.1016/S0302-4598(98)00175-5. Hope AB (January 2000). "Electron transfers amongst cytochrome f, plastocyanin and ... protein complex that uses light energy to catalyze the transfer of electrons across the thylakoid membrane from plastocyanin to ...
... is the largest subunit of cytochrome b6f complex (plastoquinol-plastocyanin reductase; EC 1.10.99.1). In its ...
An example of an entatic state is the copper center in plastocyanin, a redox enzyme. In this protein, the copper shuttles ...
Plastocyanin family of copper-binding proteins De Rienzo F, Gabdoulline RR, Menziani MC, Wade RC (August 2000). "Blue copper ...
In the second reaction, a second PQH2 gets oxidized, adding an electron to another plastocyanin and PQ. Both reactions together ... PQH2 travels to the cytochrome b6f complex which then transfers two electrons from PQH2 to plastocyanin in two separate ... is transferred to the iron-sulfur center which then transfers it to cytochrome f which then transfers it to plastocyanin. The ...
... 's spectroscopic properties help us differentiate it from plastocyanin, which is another monocopper blue protein ...
This proton pump is driven by electron transport and catalyzes the transfer of electrons from plastoquinol to plastocyanin. The ... also called plastoquinol-plastocyanin reductase) is an enzyme related to Complex III but found in the thylakoid membrane in ...
The structure is very similar to plastocyanin and azurin as they also identify as Type 1 copper proteins. They are also similar ... In class I T1Cu proteins (e.g. amicyanin, plastocyanin and pseudoazurin) the axial ligand is the sulfur of methionine, whereas ... Polarized signal-crystal absorption data on plastocyanin showed that both bands have the same polarization ratio that ... The Cysteine84 thiolate of plastocyanin accepts a hydrogen bond from a amide backbone, Asparagine38, and Histidine37 interacts ...
Plastocyanin, and Laccase. Penner-Hahn's research involves biophysical chemistry and inorganic spectroscopy including EXAFS and ...
"The unique proline of the Prochlorothrix hollandica plastocyanin hydrophobic patch impairs electron transfer to photosystem I ...
The free plastoquinone molecules eventually transfer electrons to the water-soluble plastocyanin so as to continue the light- ... The cytochrome b6f protein complex catalyzes the electron transfer between plastoquinone and plastocyanin, but also transports ... It transfers the electrons further down the electron transport chain to plastocyanin, a mobile, water-soluble electron carrier ...
Plastoquinone-plastocyanin reductase (b6f complex), present in cyanobacteria and the chloroplasts of plants, catalyses the ...
... which also share homology with the cupredoxins azurin and plastocyanin. Structurally, these domains consist of a cupredoxin- ...
The plastocyanin complex carries the electron that will neutralize the pair in the next reaction center, Photosystem I. As with ... After the electron has left Photosystem II it is transferred to a cytochrome b6f complex and then to plastocyanin, a blue ... The positive charge on the high-energy P700+ is neutralized by the transfer of an electron from plastocyanin, which receives ...
The electrons then pass through Cyt b6 and Cyt f to plastocyanin, using energy from photosystem I to pump hydrogen ions (H+) ... and finally to plastocyanin before returning to photosystem I. This transport chain produces a proton-motive force, pumping H+ ...
The excited electrons lost from the reaction center (P700) of photosystem I are replaced by transfer from plastocyanin, whose ...
... a component of the plastoquinone-plastocyanin reductase (EC 1.10.99.1), also known as the b6f complex. These complexes are ...
Cytochrome f acts as an electron donor while P700+ accepts electrons from reduced plastocyanin. Plastocyanin was the first of ... Plastocyanin (Cu2+Pc) is reduced (an electron is added) by cytochrome f according to the following reaction: Cu2+Pc + e− → Cu+ ... Plastocyanin performs electron transfer with the redox between Cu(I) and Cu(II), and it was first theorized that its entatic ... Plastocyanin is a copper-containing protein that mediates electron-transfer. It is found in a variety of plants, where it ...
Theoretical study of the electronic spectrum of plastocyanin. Kristine Pierloot, Jan O. A. De Kerpel, Ulf Ryde & Björn Roos J. ... The electronic spectrum of the blue copper protein plastocyanin has been studied by ab initio multiconfigurational second-order ...
The self-exchange rate constant (25 °C) for parsley plastocyanin is 5.0 × 104 M-1 s-1 at pH* 7.5 (I = 0.10 M). This value is ... Effect of pH on the self-exchange reactivity of the plant plastocyanin from parsley. Lookup NU author(s): Dr David Hunter, ... quite large for a higher plant plastocyanin and can be attributed to a diminished upper acidic patch in this protein. The self- ...
Photosystem I. The Light-Driven Plastocyanin: Ferredoxin Oxidoreductase. 2006. (Advances in Photosynthesis and Respiration, ...
... plastoquinol-plastocyanin oxidoreductase ; quinol cyt. c oxidoreductase (bc1) ; quinol-cytochrome c oxidoreductase complex ; ...
plastocyanin-like domain-containing protein [Arabidopsis thaliana]. Match: gi,61968968,gb,AAX57301.1,. score: 81.65. e-value: ... gi,38260640,gb,AAR15456.1, Cu2+ plastocyanin-like [Capsella rubella] Match: gi,62861389,gb,AAY16796.1,. score: 72.79. e-value: ... gi,38260606,gb,AAR15424.1, Cu2+ plastocyanin-like [Sisymbrium irio] Match: gi,21555085,gb,AAM63773.1,. score: 70.48. e-value: ... gi,38260673,gb,AAR15487.1, Cu2+ plastocyanin-like [Arabidopsis arenosa] Match: gi,218254,dbj,BAA02720.1,. score: 68.94. e-value ...
Compound: plastocyanin. Species: ANABAENA SP. [TaxId:103690]. Database cross-references and differences (RAF-indexed): *Uniprot ... Compound: plastocyanin. Species: ANABAENA SP. [TaxId:103690]. Database cross-references and differences (RAF-indexed): *Uniprot ... Keywords: electron transport, transport, beta barrel, plastocyanin, metal-binding. Deposited on 2006-03-27, released 2007-04-03 ... Description: crystal structure of plastocyanin from a cyanobacterium, anabaena variabilis. Class: electron transport. ...
Hunter DM, McFarlane W, Sykes AG, Dennison C. Effect of pH on the self-exchange reactivity of the plant plastocyanin from ... Sato K, Kohzuma T, Dennison C. Pseudospecificity of the Acidic Patch of Plastocyanin for the Interaction with Cytochrome f. ... Dennison C, Sato K. Paramagnetic 1H NMR Spectrum of the Cobalt(II) Derivative of Spinach Plastocyanin. Inorganic Chemistry 2004 ... Crowley PB, Hunter DM, Sato K, McFarlane W, Dennison C. The parsley plastocyanin-turnip cytochrome f complex: A structurally ...
Plastoquinol-plastocyanin reductase A completely distinct family of cytochromes are known as the cytochrome P450 oxidases, so ...
Copper and iron metabolism in Ostreococcus tauri - the role of phytotransferrin, plastocyanin and a chloroplast copper- ...
Gorman, D. S. & Levine, R. P. Cytochrome F and plastocyanin - Their sequence in photosynthetic electron transport chain of ...
Gorman, D. S., and Levine, R. P. (1965). Cytochrome F and plastocyanin: their sequence in the photosynthetic electron transport ...
b.6.1.1: Plastocyanin/azurin-like [49504] (8 proteins). mono-domain proteins. ...
blue copper proteins, e.g. plastocyanin, nitrite reducates, and azurin. *Mo enzymes (DMSO reductase, sulfite oxidase, xanthine ...
The cytochrome f - plastocyanin complex as a model to study transient interactions between redox proteins. FEBS Letters. 2012. ... TRANSIENT BINDING OF PLASTOCYANIN TO ITS PHYSIOLOGICAL REDOX PARTNERS MODIFIES THE COPPER SITE GEOMETRY. FEBS Letters. 2006. ... CYTOCHROME C6 AND PLASTOCYANIN: THEIR STRUCTURAL AND FUNCTIONAL SIMILARITIES MAKE BOTH PROTEINS PLAY THE SAME PHYSIOLOGICAL ... CYTOCHROME C6 AND PLASTOCYANIN: THEIR STRUCTURAL AND FUNCTIONAL SIMILARITIES MAKE BOTH PROTEINS PLAY THE SAME PHYSIOLOGICAL ...
Plastocyanin contains a copper ion (Cu) bound to four amino acids. His37, Cys84, His87 and Met92. We will need to modify these ... In this tutorial we will be aiming to setup a protein simulation of Plastocyanin in explicit solvent. In order to do this there ... Using the most probable protonation states (at neutral pH) results in the Plastocyanin protein having an overall charge of -9. ... The PDB file for plastocyanin (1PLC) contains crystallographic waters which we should keep. However, only the oxygen positions ...
Schöttler, M. A.; Kirchhoff, H.; Weis, E.: The role of plastocyanin in the adjustment of the photosynthetic electron transport ... Kirchhoff, H.; Schöttler, M. A.; Maurer, J.; Weis, E.: Plastocyanin redox kinetics in spinach chloroplasts: evidence for ...
Plastocyanin content in rice leaves treated with 0.125 mg/liter manganese Rice Oryza sativa. 1.23. mmol/umol chlorophyll. ...
Sommer, F., F. Drepper and M. Hippler (2002). The luminal helix l of PsaB is essential for recognition of plastocyanin or ...
... but not for plastocyanin oxidation in tobacco. Biochemical Journal 403 (2), S. 251 - 260 (2007) ...
Boekema, E. J., Kouril, R., Dekker, J. P. & Jensen, Poul Erik, 2006, Photosystem I: the light-driven plastocyanin: ferredoxin ...
... poplar plastocyanin at six pH values," Journal of Molecular Biology, vol. 192, no. 2, pp. 361-387, 1986. ...
... and plastocyanin (cytochrome c6 ), we found other genes utilizing the same strategy involved in nitrogen assimilation and fatty ...
The protein plastocyanin (Pc) is responsible for shuttling electrons between two of these protein complexes in the ... and plastocyanin (Pc) under illumination and redox control (oxidized, reduced). Example quantification of unbinding forces ... and Redox-Dependent Force Spectroscopy Reveals that the Interaction between Plastocyanin and Plant Photosystem I Is Favored ...
One example of this is the metalloprotein plastocyanin, which has a copper atom at its centre and is responsible for important ...
plastoquinol-plastocyanin reductase. -. 7e+0. At5g11990. proline-rich family protein. S.X.. H.G.. Please select. ...
In particular, the decrease in plastocyanin and ferredoxin-NADP reductase suggests that H2O2 accumulation is associated with ... After 35 d under Low S conditions, we observed: 1, a repression of ferredoxin-NADP reductase (FNR) and plastocyanin (PC) (Table ... In particular, the decrease in plastocyanin and ferredoxin-NADP reductase suggests that H2O2 accumulation is associated with ... In contrast, two proteins that belong to the electron transfer chain in the thylakoidal membrane were repressed: plastocyanin ( ...
In J. H. Golbeck (Ed.), Photosystem I: The Light-Driven, Plastocyanin:Ferredoxin Oxidoreductase (pp. 177-192). Springer. ... in JH Golbeck (ed.), Photosystem I: The Light-Driven, Plastocyanin:Ferredoxin Oxidoreductase. Springer, The Netherlands, pp. ... Photosystem I: The Light-Driven, Plastocyanin:Ferredoxin Oxidoreductase. ed. / J.H. Golbeck. The Netherlands: Springer, 2006. p ... Photosystem I: The Light-Driven, Plastocyanin:Ferredoxin Oxidoreductase. editor / J.H. Golbeck. The Netherlands : Springer, ...
plastocyanin-like domain-containing protein. F:electron carrier activity, copper ion binding;P:unknown;C:anchored to membrane; ...
Photoinduced Electron-Transfer within Complexes between Plastocyanin and Ruthenium Bisbipyridine Dicarboxybipyridine Cytochrome ... Photoinduced Electron-Transfer within Complexes between Plastocyanin and Ruthenium Bisbipyridine Dicarboxybipyridine Cytochrome ...
  • In photosynthesis, plastocyanin functions as an electron transfer agent between cytochrome f of the cytochrome b6f complex from photosystem II and P700+ from photosystem I. Cytochrome b6f complex and P700+ are both membrane-bound proteins with exposed residues on the lumen-side of the thylakoid membrane of chloroplasts. (wikipedia.org)
  • Plastocyanin was the first of the blue copper proteins to be characterised by X-ray crystallography. (wikipedia.org)
  • Cytochrome f acts as an electron donor while P700+ accepts electrons from reduced plastocyanin. (wikipedia.org)
  • Plastocyanin (Cu2+Pc) is reduced (an electron is added) by cytochrome f according to the following reaction: Cu2+Pc + e− → Cu+Pc After dissociation, Cu+Pc diffuses through the lumen space until recognition/binding occurs with P700+, at which point P700+ oxidizes Cu+Pc according to the following reaction: Cu+Pc → Cu2+Pc + e− The redox potential is about 370 mV and the isoelectric pH is about 4. (wikipedia.org)
  • In addition to typical substitution responses from an iron-economic toward an iron-sufficient state for flavodoxin (ferredoxin) and plastocyanin (cytochrome c 6 ), we found other genes utilizing the same strategy involved in nitrogen assimilation and fatty acid desaturation. (nih.gov)
  • Plastocyanin is a "blue" copper protein which catalyzes electron transfer between the cytochrome b6 .f complex and P-700, the reaction center of photosystem I. Plastocyanin is a nuclear encoded polypeptide in all eukaryotic photosynthetic organisms where it has been studied. (agrisera.com)
  • A protease-mediated mechanism handles the cytochrome c6/plastocyanin swap throughout Synechocystis sp. (mirnamimic.com)
  • The electronic spectrum of the blue copper protein plastocyanin has been studied by ab initio multiconfigurational second-order perturbation theory (the CASPT2 method). (lu.se)
  • The protein plastocyanin (Pc) is responsible for shuttling electrons between two of these protein complexes in the photosynthetic electron transport chain. (icrea.cat)
  • Plastocyanin works more on the principles of entatic states where it increases the energy of the reactants, decreasing the amount of energy needed for the redox reaction to occur. (wikipedia.org)
  • To study the properties of the redox reaction of plastocyanin, methods such as quantum mechanics / molecular mechanics (QM/MM) molecular dynamics simulations. (wikipedia.org)
  • Plastocyanin performs electron transfer with the redox between Cu(I) and Cu(II), and it was first theorized that its entatic state was a result of the protein imposing an undistorted tetrahedral geometry preferred by ordinary Cu(I) complexes onto the oxidized Cu(II) site. (wikipedia.org)
  • Plastocyanin redox kinetics in spinach chloroplasts: evidence for disequilibrium in the high potential chain. (mpg.de)
  • Single molecule force spectroscopy setup to evaluate interactions between partners photosynthetic complex I (PSI) and plastocyanin (Pc) under illumination and redox control (oxidized, reduced). (icrea.cat)
  • Plastocyanin is a copper-containing protein that mediates electron-transfer. (wikipedia.org)
  • Four-coordinate copper complexes often exhibit square planar geometry, however plastocyanin has a trigonally distorted tetrahedral geometry. (wikipedia.org)
  • Plastocyanin contains a copper ion (Cu) bound to four amino acids. (ambermd.org)
  • One example of this is the metalloprotein plastocyanin, which has a copper atom at its centre and is responsible for important steps in the transfer of electrons during photosynthesis. (lightsources.org)
  • Photosystem I. The Light-Driven Plastocyanin: Ferredoxin Oxidoreductase. (koeltz.com)
  • In particular, the decrease in plastocyanin and ferredoxin-NADP reductase suggests that H 2 O 2 accumulation is associated with perturbation of the photosynthetic electron transport chain. (biomedcentral.com)
  • The long-wavelength chlorophylls of photosystem I . In J. H. Golbeck (Ed.), Photosystem I: The Light-Driven, Plastocyanin:Ferredoxin Oxidoreductase (pp. 177-192). (vu.nl)
  • The role of plastocyanin in the adjustment of the photosynthetic electron transport to the carbon metabolism in tobacco. (mpg.de)
  • Plastocyanin is indispensable for photosynthetic electron flow in Arabidopsis thaliana. (mpg.de)
  • Plastocyanin, chloroplast precursor. (go.jp)
  • The plastome-encoded PsaJ subunit is required for efficient Photosystem I excitation, but not for plastocyanin oxidation in tobacco. (mpg.de)
  • 1996). Molecular genetic analysis of plastocyanin biosynthesis in Chlamydomonas reinhardtii. (agrisera.com)
  • Molekulargenetische und physiologische Analysen von Plastocyanin and Cytochrom Cx-Mutanten bei Arabidopsis thaliana. (mpg.de)
  • In this tutorial we will be aiming to setup a protein simulation of Plastocyanin in explicit solvent. (ambermd.org)
  • Plastocyanin is believed to work less like an enzyme where enzymes decrease the transition energy needed to transfer the electron. (wikipedia.org)
  • Photosystem I (PSI) is a multisubunit pigment-protein complex that uses light energy to transfer electrons from plastocyanin to ferredoxin. (elsevierpure.com)
  • The photosystem that makes use of light to transfer electron particualrly from plastocyanin to ferredoxin, and whose reaction center chlorophyll is P700. (biologyonline.com)
  • In cyclic electron flow , the electron begins in a pigment complex called photosystem I, passes from the primary acceptor to ferredoxin , then to cytochrome b6f (a similar complex to that found in mitochondria), and then to plastocyanin before returning to chlorophyll. (en-academic.com)
  • Klas-NIR spectrophotometer has been lately developed by Klughammer and Schreiber (Photosynth Res 128:195-214, 2016) for in vivo measurements of redox modifications of P700, plastocyanin (Pcy) and ferredoxin (Fd). (unicoupi.com)
  • PsaF (PSI-F subunit of photosystem I ) is a plastocyanin-docking protein, involved in electron transfer from plastocyanin to c553. (agrisera.com)
  • The mutations replaced the loop containing three (Cys93, His96, Met99) of the four copper ligands in amicyanin by the 'ligand loops' of P. aeruginosa azurin (AmiAzu), A. faecalis pseudoazurin (AmiPaz), P. nigra plastocyanin (AmiPcy), and P. aureofaciens nitrite reductase (AmiNiR). (ncl.ac.uk)
  • Plastocyanin redox kinetics in spinach chloroplasts: evidence for disequilibrium in the high potential chain. (mpg.de)
  • The role of plastocyanin in the adjustment of the photosynthetic electron transport to the carbon metabolism in tobacco. (mpg.de)
  • Plastocyanin is a copper-containing protein that mediates electron-transfer. (wikipedia.org)
  • Four-coordinate copper complexes often exhibit square planar geometry, however plastocyanin has a trigonally distorted tetrahedral geometry. (wikipedia.org)
  • Plastocyanin performs electron transfer with the redox between Cu(I) and Cu(II), and it was first theorized that its entatic state was a result of the protein imposing an undistorted tetrahedral geometry preferred by ordinary Cu(I) complexes onto the oxidized Cu(II) site. (wikipedia.org)
  • 7. Photo processes on self-associated cationic porphyrins and plastocyanin complexes 1. (nih.gov)
  • Plastocyanin works more on the principles of entatic states where it increases the energy of the reactants, decreasing the amount of energy needed for the redox reaction to occur. (wikipedia.org)
  • Another way to rephrase the function of plastocyanin is that it can facilitate the electron transfer reaction by providing a small reorganization energy, which has been measured to about 16-28 kcal/mol (67-117 kJ/mol). (wikipedia.org)
  • abstract = "The reactivity of plastocyanin from a green algal source, Scenedesmus obliquus (estimated PCuI charge -9 at pH ~7), has been studied for the first time in order to further assess the effect of amino acid sequence variations in naturally occurring plastocyanins. (tees.ac.uk)
  • Moreover, phenotypic analysis of atc6-1 pete1 and atc6-1 pete2 double mutants, each lacking Cyt c(6A) and one of the two plastocyanin-encoding genes, failed to reveal any genetic interaction. (uni-muenchen.de)
  • Plastocyanin is believed to work less like an enzyme where enzymes decrease the transition energy needed to transfer the electron. (wikipedia.org)
  • Ligation of plastocyanin tyrosine 83 onto metalloporphyrins and electron-transfer fluorescence quenching. (nih.gov)
  • Overexpression of either PETE1 or PETE2 in the pete1 pete2 double knockout mutant background results in essentially wild-type photosynthetic performance, excluding the possibility that the two plastocyanin isoforms could have distinct functions in thylakoid electron flow. (uni-muenchen.de)
  • This method was used to determine that plastocyanin has an entatic strain energy of about 10 kcal/mol (42 kJ/mol). (wikipedia.org)