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Water Splitting
Water splitting is the chemical reaction in which water is broken down into oxygen and hydrogen: Efficient and economical water splitting would be a technological breakthrough that could underpin a hydrogen economy. A version of water splitting occurs in photosynthesis, but hydrogen is not produced. The reverse of water splitting is the basis of the hydrogen fuel cell. Water splitting using solar radiation has not been commercialized. Electrolysis Electrolysis of water is the decomposition of water (H2O) into oxygen (O2) and hydrogen (H2): Production of hydrogen from water is energy intensive. Usually, the electricity consumed is more valuable than the hydrogen produced, so this method has not been widely used. In contrast with low-temperature electrolysis, high-temperature electrolysis (HTE) of water converts more of the initial heat energy into chemical energy (hydrogen), potentially doubling efficiency to about 50%. Because some of the energy in HTE is supplied in th ...
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Electrolysis Of Water
Electrolysis of water is using electricity to Water splitting, split water into oxygen () and hydrogen () gas by electrolysis. Hydrogen gas released in this way can be used as hydrogen fuel, but must be kept apart from the oxygen as the mixture would be extremely explosive. Separately pressurised into convenient 'tanks' or 'gas bottles', hydrogen can be used for oxyhydrogen welding and other applications, as the hydrogen / oxygen flame can reach approximately 2,800°C. Water electrolysis requires a minimum potential difference of 1.23 volts, although at that voltage external heat is also required. Typically 1.5 volts is required. Electrolysis is rare in industrial applications since hydrogen can be produced less expensively from fossil fuels. Most of the time, hydrogen is made by splitting methane (CH4) into carbon dioxide (CO2) and hydrogen (H2) via steam reforming. This is a carbon-intensive process that means for every kilogram of “grey” hydrogen produced, approximatel ...
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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 ...
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Bioreactor
A bioreactor is any manufactured device or system that supports a biologically active environment. In one case, a bioreactor is a vessel in which a chemical reaction, chemical process is carried out which involves organisms or biochemistry, biochemically active chemical substance, substances derived from such organisms. This process can either be Aerobic organism, aerobic or Anaerobic organism, anaerobic. These bioreactors are commonly cylindrical, ranging in size from litres to cubic metres, and are often made of stainless steel. It may also refer to a device or system designed to grow Cell (biology), cells or Biological tissue, tissues in the context of cell culture. These devices are being developed for use in tissue engineering or biochemical engineering, biochemical/bioprocess engineering, bioprocess engineering. On the basis of mode of operation, a bioreactor may be classified as batch reactor, batch, fed-batch, fed batch or continuous reactor, continuous (e.g. a continuous s ...
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Biohydrogen
Biohydrogen is hydrogen, H2 that is produced biologically. Interest is high in this technology because H2 is a clean fuel and can be readily produced from certain kinds of biomass, including biological waste. Furthermore some photosynthetic microorganisms are capable to produce H2 directly from water splitting using light as energy source. Besides the promising possibilities of biological hydrogen production, many challenges characterize this technology. First challenges include those intrinsic to H2, such as storage and transportation of an explosive noncondensible gas. Additionally, hydrogen producing organisms are Oxidative stress, poisoned by O2 and yields of H2 are often low. Biochemical principles The main reactions driving hydrogen formation involve the oxidation of substrates to obtain electrons. Then, these electrons are transferred to free protons to form molecular hydrogen. This proton reduction reaction is normally performed by an enzyme family known as hydrogenases. ...
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Hydrogenase
A hydrogenase is an enzyme that Catalysis, catalyses the reversible Redox, oxidation of molecular hydrogen (H2), as shown below: Hydrogen oxidation () is coupled to the reduction of electron acceptors such as oxygen, nitrate, Ferric, ferric ion, sulfate, carbon dioxide (), and fumarate. On the other hand, proton reduction () is coupled to the oxidation of electron donors such as ferredoxin (FNR), and serves to dispose excess electrons in cells (essential in pyruvate fermentation). Both low-molecular weight compounds and proteins such as FNRs, cytochrome ''c''3, and cytochrome ''c''6 can act as physiological electron donors or acceptors for hydrogenases. Structural classification It has been estimated that 99% of all organisms utilize hydrogen, H2. Most of these species are microbes and their ability to use H2 as a metabolite arises from the expression of metalloenzymes known as hydrogenases. Hydrogenases are sub-classified into three different types based on the active site ...
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Biological Hydrogen Production (Algae)
Biohydrogen is H2 that is produced biologically. Interest is high in this technology because H2 is a clean fuel and can be readily produced from certain kinds of biomass, including biological waste. Furthermore some photosynthetic microorganisms are capable to produce H2 directly from water splitting using light as energy source. Besides the promising possibilities of biological hydrogen production, many challenges characterize this technology. First challenges include those intrinsic to H2, such as storage and transportation of an explosive noncondensible gas. Additionally, hydrogen producing organisms are poisoned by O2 and yields of H2 are often low. Biochemical principles The main reactions driving hydrogen formation involve the oxidation of substrates to obtain electrons. Then, these electrons are transferred to free protons to form molecular hydrogen. This proton reduction reaction is normally performed by an enzyme family known as hydrogenases. In heterotrophic organi ...
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Algae Hydrogen Production
Algae ( , ; : alga ) is an informal term for any organisms of a large and diverse group of photosynthetic organisms that are not plants, and includes species from multiple distinct clades. Such organisms range from unicellular microalgae, such as cyanobacteria, ''Chlorella'', and diatoms, to multicellular macroalgae such as kelp or brown algae which may grow up to in length. Most algae are aquatic organisms and lack many of the distinct cell and tissue types, such as stomata, xylem, and phloem that are found in land plants. The largest and most complex marine algae are called seaweeds. In contrast, the most complex freshwater forms are the Charophyta, a division of green algae which includes, for example, ''Spirogyra'' and stoneworts. Algae that are carried passively by water are plankton, specifically phytoplankton. Algae constitute a polyphyletic group because they do not include a common ancestor, and although eukaryotic algae with chlorophyll-bearing plastids seem to ha ...
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Manganese
Manganese is a chemical element; it has Symbol (chemistry), symbol Mn and atomic number 25. It is a hard, brittle, silvery metal, often found in minerals in combination with iron. Manganese was first isolated in the 1770s. It is a transition metal with a multifaceted array of industrial alloy uses, particularly in stainless steels. It improves strength, workability, and resistance to wear. Manganese oxide is used as an oxidising agent, as a rubber additive, and in glass making, fertilisers, and ceramics. Manganese sulfate can be used as a fungicide. Manganese is also an essential human dietary element, important in macronutrient metabolism, bone formation, and free radical defense systems. It is a critical component in dozens of proteins and enzymes. It is found mostly in the bones, but also the liver, kidneys, and brain. In the human brain, the manganese is bound to manganese metalloproteins, most notably glutamine synthetase in astrocytes. Manganese is commonly found in labo ...
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Active Site
In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the ''binding site'', and residues that catalyse a reaction of that substrate, the ''catalytic site''. Although the active site occupies only ~10–20% of the volume of an enzyme, it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes. Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their functio ...
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Oxygen-evolving Complex
The oxygen-evolving complex (OEC), also known as the water-splitting complex, is a water-oxidizing enzyme involved in the photo-oxidation of water during the light reactions of photosynthesis. OEC is surrounded by 4 core proteins of photosystem II at the membrane-lumen interface. The mechanism for splitting water involves absorption of three photons before the fourth provides sufficient energy for water oxidation. Based on a widely accepted theory from 1970 by Kok, the complex can exist in 5 states, denoted S0 to S4, with S0 the most reduced and S4 the most oxidized. Energy from the photons captured by photosystem II moves the system from state S0 to S1 to S2 to S3 and finally to S4. S4 reacts with water producing free oxygen: : This conversion resets the catalyst to the S0 state. The active site of the OEC consists of a cluster of manganese and calcium with the formula Mn4Ca1OxCl1–2(HCO3)y. This cluster is bound to D1 and CP43 subunits and stabilized by peripheral membrane ...
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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 ...
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Cytochrome
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 na ...
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