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Saturday, 31 May 2014
Friday, 18 April 2014
Tuesday, 1 April 2014
Hydrolysis
Hydrolysis usually means the cleavage of chemical bonds by the addition of water. Where a carbohydrate is broken into its component sugar molecules by hydrolysis (e.g. sucrose being broken down into glucose and fructose), this is termed saccharification. Generally, hydrolysis or saccharification is a step in the degradation of a substance.
Strong acids also undergo hydrolysis. For example, dissolving sulfuric acid (H2SO4) in water is accompanied by hydrolysis to give hydronium and bisulfate, the sulfuric acid's conjugate base. For a more technical discussion of what occurs during such a hydrolysis, see Brønsted–Lowry acid–base theory.
Perhaps the oldest commercially practiced example of ester hydrolysis is saponification (formation of soap). It is the hydrolysis of a triglyceride (fat) with an aqueous base such as sodium hydroxide (NaOH). During the process, glycerol is formed, and the fatty acids react with the base, converting them to salts. These salts are called soaps, commonly used in households.
In addition, in living systems, most biochemical reactions (including ATP hydrolysis) take place during the catalysis of enzymes. The catalytic action of enzymes allows the hydrolysis of proteins, fats, oils, and carbohydrates. As an example, one may consider proteases (enzymes that aid digestion by causing hydrolysis of peptide bonds in proteins). They catalyse the hydrolysis of interior peptide bonds in peptide chains, as opposed to exopeptidases (another class of enzymes, that catalyse the hydrolysis of terminal peptide bonds, liberating one free amino acid at a time).
However, proteases do not catalyse the hydrolysis of all kinds of proteins. Their action is stereo-selective: Only proteins with a certain tertiary structure are targeted as some kind of orienting force is needed to place the amide group in the proper position for catalysis. The necessary contacts between an enzyme and its substrates (proteins) are created because the enzyme folds in such a way as to form a crevice into which the substrate fits; the crevice also contains the catalytic groups. Therefore, proteins that do not fit into the crevice will not undergo hydrolysis. This specificity preserves the integrity of other proteins such as hormones, and therefore the biological system continues to function normally.
Upon hydrolysis, an amide converts into a carboxylic acid and an amine or ammonia. The carboxylic acid has a hydroxyl group derived from a water molecule and the amine (or ammonia) gains the hydrogen ion. The hydrolysis of peptides gives amino acids.
Many polyamide polymers such as nylon 6,6 hydrolyse in the presence of strong acids. The process leads to depolymerization. For this reason nylon products fail by fracturing when exposed to small amounts of acidic water. Polyesters are also susceptible to similar polymer degradation reactions. The problem is known as stress corrosion cracking.
Monosaccharides can be linked together by glycosidic bonds, which can be cleaved by hydrolysis. Two, three, several or many monosaccharides thus linked form disaccharides, trisaccharides, oligosaccharides or polysaccharides, respectively. Enzymes that hydrolyse glycosidic bonds are called "glycoside hydrolases" or "glycosidases".
The best-known disaccharide is sucrose (table sugar). Hydrolysis of sucrose yields glucose and fructose. Invertase is a sucrase used industrially for the hydrolysis of sucrose to so-called invert sugar. Lactase is essential for digestive hydrolysis of lactose in milk; many adult humans do not produce lactase and cannot digest the lactose in milk (not a disorder).
The hydrolysis of polysaccharides to soluble sugars is called "saccharification". Malt made from barley is used as a source of β-amylase to break down starch into the disaccharide maltose, which can be used by yeast to produce beer. Other amylase enzymes may convert starch to glucose or to oligosaccharides. Cellulose is first hydrolyzed to cellobiose by cellulase and then cellobiose is further hydrolyzed to glucose by beta-glucosidase. Animals such as cows (ruminants) are able to hydrolyze cellulose into cellobiose and then glucose because of symbiotic bacteria that produce cellulases.
The dissociation constant, pKa, for this reaction is more or less linearly related to the charge-to-size ratio of the metal ion. Ions with low charges, such as Na+ are very weak acids with almost imperceptible hydrolysis. Large divalent ions such as Ca2+, Zn2+, Sn2+ and Pb2+ have a pKa of 6 or more and would not normally be classed as acids, but small divalent ions such as Be2+ undergo extensive hydrolysis. Trivalent ions like Al3+ and Fe3+ are weak acids whose pKa is comparable to that of acetic acid. Solutions of salts such as BeCl2 or Al(NO3)3 in water are noticeably acidic; the hydrolysis can be suppressed by adding an acid such as nitric acid, making the solution more acidic.
Hydrolysis may proceed beyond the first step, often with the formation of polynuclear species via the process of olation. Some "exotic" species such as Sn3(OH)42+ are well characterized. Hydrolysis tends to proceed as pH rises leading, in many cases, to the precipitation of a hydroxide such as Al(OH)3 or AlO(OH). These substances, major constituents of bauxite, are known as laterites and are formed by leaching from rocks of most of the ions other than aluminium and iron and subsequent hydrolysis of the remaining aluminium and iron.
Types
Usually hydrolysis is a chemical process in which a molecule of water is added to a substance. Sometimes this addition causes both substance and water molecule to split into two parts. In such reactions, one fragment of the target molecule (or parent molecule) gains a hydrogen ion.Salts
A common kind of hydrolysis occurs when a salt of a weak acid or weak base (or both) is dissolved in water. Water spontaneously ionizes into hydroxide anions and hydrogen cations. The salt, too, dissociates into its constituent anions and cations. For example, sodium acetate dissociates in water into sodium and acetate ions. Sodium ions react very little with the hydroxide ions whereas the acetate ions combine with hydrogen ions to produce acetic acid. In this case the net result is a relative excess of hydroxide ions, giving a basic solution.Strong acids also undergo hydrolysis. For example, dissolving sulfuric acid (H2SO4) in water is accompanied by hydrolysis to give hydronium and bisulfate, the sulfuric acid's conjugate base. For a more technical discussion of what occurs during such a hydrolysis, see Brønsted–Lowry acid–base theory.
Esters and amides
Acid–base-catalysed hydrolyses are very common; one example is the hydrolysis of amides or esters. Their hydrolysis occurs when the nucleophile (a nucleus-seeking agent, e.g., water or hydroxyl ion) attacks the carbon of the carbonyl group of the ester or amide. In an aqueous base, hydroxyl ions are better nucleophiles than polar molecules such as water. In acids, the carbonyl group becomes protonated, and this leads to a much easier nucleophilic attack. The products for both hydrolyses are compounds with carboxylic acid groups.Perhaps the oldest commercially practiced example of ester hydrolysis is saponification (formation of soap). It is the hydrolysis of a triglyceride (fat) with an aqueous base such as sodium hydroxide (NaOH). During the process, glycerol is formed, and the fatty acids react with the base, converting them to salts. These salts are called soaps, commonly used in households.
In addition, in living systems, most biochemical reactions (including ATP hydrolysis) take place during the catalysis of enzymes. The catalytic action of enzymes allows the hydrolysis of proteins, fats, oils, and carbohydrates. As an example, one may consider proteases (enzymes that aid digestion by causing hydrolysis of peptide bonds in proteins). They catalyse the hydrolysis of interior peptide bonds in peptide chains, as opposed to exopeptidases (another class of enzymes, that catalyse the hydrolysis of terminal peptide bonds, liberating one free amino acid at a time).
However, proteases do not catalyse the hydrolysis of all kinds of proteins. Their action is stereo-selective: Only proteins with a certain tertiary structure are targeted as some kind of orienting force is needed to place the amide group in the proper position for catalysis. The necessary contacts between an enzyme and its substrates (proteins) are created because the enzyme folds in such a way as to form a crevice into which the substrate fits; the crevice also contains the catalytic groups. Therefore, proteins that do not fit into the crevice will not undergo hydrolysis. This specificity preserves the integrity of other proteins such as hormones, and therefore the biological system continues to function normally.
Upon hydrolysis, an amide converts into a carboxylic acid and an amine or ammonia. The carboxylic acid has a hydroxyl group derived from a water molecule and the amine (or ammonia) gains the hydrogen ion. The hydrolysis of peptides gives amino acids.
Many polyamide polymers such as nylon 6,6 hydrolyse in the presence of strong acids. The process leads to depolymerization. For this reason nylon products fail by fracturing when exposed to small amounts of acidic water. Polyesters are also susceptible to similar polymer degradation reactions. The problem is known as stress corrosion cracking.
ATP
Hydrolysis is related to energy metabolism and storage. All living cells require a continual supply of energy for two main purposes: for the biosynthesis of micro and macromolecules, and for the active transport of ions and molecules across cell membranes. The energy derived from the oxidation of nutrients is not used directly but, by means of a complex and long sequence of reactions, it is channelled into a special energy-storage molecule, adenosine triphosphate (ATP). The ATP molecule contains pyrophosphate linkages (bonds formed when two phosphate units are combined together) that release energy when needed. ATP can undergo hydrolysis in two ways: the removal of terminal phosphate to form adenosine diphosphate (ADP) and inorganic phosphate, or the removal of a terminal diphosphate to yield adenosine monophosphate (AMP) and pyrophosphate. The latter usually undergoes further cleavage into its two constituent phosphates. This results in biosynthesis reactions, which usually occur in chains, that can be driven in the direction of synthesis when the phosphate bonds have undergone hydrolysis.Polysaccharides
The best-known disaccharide is sucrose (table sugar). Hydrolysis of sucrose yields glucose and fructose. Invertase is a sucrase used industrially for the hydrolysis of sucrose to so-called invert sugar. Lactase is essential for digestive hydrolysis of lactose in milk; many adult humans do not produce lactase and cannot digest the lactose in milk (not a disorder).
The hydrolysis of polysaccharides to soluble sugars is called "saccharification". Malt made from barley is used as a source of β-amylase to break down starch into the disaccharide maltose, which can be used by yeast to produce beer. Other amylase enzymes may convert starch to glucose or to oligosaccharides. Cellulose is first hydrolyzed to cellobiose by cellulase and then cellobiose is further hydrolyzed to glucose by beta-glucosidase. Animals such as cows (ruminants) are able to hydrolyze cellulose into cellobiose and then glucose because of symbiotic bacteria that produce cellulases.
Metal aqua ions
Metal ions are Lewis acids, and in aqueous solution they form aqua ions of the general formula M(H2O)nm+. The aqua ions undergo hydrolysis, to a greater or lesser extent. The first hydrolysis step is given generically as- M(H2O)nm+ + H2O
M(H2O)n−1(OH)(m−1)+ + H3O+
The dissociation constant, pKa, for this reaction is more or less linearly related to the charge-to-size ratio of the metal ion. Ions with low charges, such as Na+ are very weak acids with almost imperceptible hydrolysis. Large divalent ions such as Ca2+, Zn2+, Sn2+ and Pb2+ have a pKa of 6 or more and would not normally be classed as acids, but small divalent ions such as Be2+ undergo extensive hydrolysis. Trivalent ions like Al3+ and Fe3+ are weak acids whose pKa is comparable to that of acetic acid. Solutions of salts such as BeCl2 or Al(NO3)3 in water are noticeably acidic; the hydrolysis can be suppressed by adding an acid such as nitric acid, making the solution more acidic.
Hydrolysis may proceed beyond the first step, often with the formation of polynuclear species via the process of olation. Some "exotic" species such as Sn3(OH)42+ are well characterized. Hydrolysis tends to proceed as pH rises leading, in many cases, to the precipitation of a hydroxide such as Al(OH)3 or AlO(OH). These substances, major constituents of bauxite, are known as laterites and are formed by leaching from rocks of most of the ions other than aluminium and iron and subsequent hydrolysis of the remaining aluminium and iron.
Saturday, 15 March 2014
Reference Electrode
A reference electrode is an electrode which has a stable and well-known electrode potential. The high stability of the electrode potential is usually reached by employing a redox system with constant (buffered or saturated) concentrations of each participants of the redox reaction.
There are many ways reference electrodes are used. The simplest is when the reference electrode is used as a half cell to build an electrochemical cell. This allows the potential of the other half cell to be determined. An accurate and practical method to measure an electrode's potential in isolation (absolute electrode potential) has yet to be developed.
The potential for the Fc0/+ couple is sensitive to solvent.
A Quasi-Reference Electrode (QRE) avoids the issues mentioned above. A QRE with ferrocene or similar internal standard (cobaltocene)
referenced back to ferrocene is ideal for nonaqueous work. Since the
early 1960s ferrocene has been gaining acceptance as the standard
reference for nonaqueous work for a number of reasons, and in 1984,
IUPAC recommended ferrocene (II/III) as a standard redox couple.
The preparation of the QRE electrode is simple, allowing for a fresh
reference to be prepared with each set of experiments. Since QREs are
made fresh, there is also no concern with improper storage or
maintenance of the electrode. QREs are also more affordable than other
reference electrodes.
To make a quasi-reference electrode (QRE):
Yttria-stabilized zirconia (YSZ) membrane electrodes were developed with a variety of redox couples, e.g., Ni/NiO. Their potential depends on pH. When the pH value is known, these electrodes can be employed as a reference with notable applications at elevated temperatures.
There are many ways reference electrodes are used. The simplest is when the reference electrode is used as a half cell to build an electrochemical cell. This allows the potential of the other half cell to be determined. An accurate and practical method to measure an electrode's potential in isolation (absolute electrode potential) has yet to be developed.
Aqueous reference electrodes
Common reference electrodes and potential with respect to the standard hydrogen electrode:- Standard hydrogen electrode (SHE) (E=0.000 V) activity of H+=1
- Normal hydrogen electrode (NHE) (E ≈ 0.000 V)concentration H+=1
- Reversible hydrogen electrode (RHE) (E=0.000 V - 0.0591*pH)
- Saturated calomel electrode (SCE) (E=+0.241 V saturated)
- Copper-copper(II) sulfate electrode(CSE) (E=+0.314 V)
- Silver chloride electrode (E=+0.197 V saturated)
- pH-electrode (in case of pH buffered solutions, see buffer solution)
- Palladium-hydrogen electrode
- Dynamic hydrogen electrode (DHE)
-
Standard Hydrogen Electrode
-
Cu-Cu(II) reference electrode
-
Ag-AgCl reference electrode
Nonaqueous reference electrodes
While it is convenient to compare between solvents to qualitatively compare systems it is not quantitatively meaningful. Much as pKa are related between solvents, but not the same, so is the case with E°. While the SHE might seem to be a reasonable reference for nonaqueous work as it turns out the platinum is rapidly poisoned by many solvents including acetonitrile causing uncontrolled drifts in potential. Both the SCE and saturated Ag/AgCl are aqueous electrodes based around saturated aqueous solution. While for short periods it may be possible to use such aqueous electrodes as references with nonaqueous solutions the long-term results are not trustworthy. Using aqueous electrodes introduces undefined, variable, and unmeasurable junction potentials to the cell in the form of a liquid-liquid junction as well as different ionic composition between the reference compartment and the rest of the cell. The best argument against using aqueous reference electrodes with nonaqueous systems, as mentioned earlier, is that potentials measured in different solvents are not directly comparable.The potential for the Fc0/+ couple is sensitive to solvent.
| Fc0/+ couple, NBu4PF6 at 298 °C | |
|---|---|
| solvent | E |
| MeCN | 0.40 |
| CH2Cl2 | 0.46 |
| THF | 0.56 |
| DMF | 0.45 |
| acetone | 0.48 |
To make a quasi-reference electrode (QRE):
- Insert a piece of silver wire into concentrated HCl then allow the wire to dry on a KimWipe. This forms an insoluble layer of AgCl on the surface of the electrode and gives you a Ag/AgCl wire. Repeat dipping every few months or if the QRE starts to drift.
- Obtain a Vycor glass frit (4 mm diameter) and glass tubing of similar diameter. Attach Vycor glass frit to the glass tubing with heat shrink Teflon tubing.
- Rinse then fill the clean glass tube with supporting electrolyte solution and insert Ag/AgCl wire.
- The ferrocene (II/III) couple should lie around 400 mV versus this Ag/AgCl QRE in an acetonitrile solution. This potential will varying up to 200 mV with the specific undefined conditions. Thus adding an internal standard such as ferrocene at some point during the experiment is always necessary.
Pseudo-reference electrodes
A pseudo-reference electrode is a term that is not well defined and borders on having multiple meanings since pseudo and quasi are often used interchangeably. They are a class of electrodes named pseudo-reference electrodes because they do not maintain a constant potential but vary predictably with conditions. If the conditions are known, the potential can be calculated and the electrode can be used as a reference. Most electrodes work over a limited range of conditions, such as pH or temperature, outside of this range the electrodes behavior becomes unpredictable. The advantage of a pseudo-reference electrode is that the resulting variation is factored into the system allowing researchers to accurately study systems over a wide range of conditions.Yttria-stabilized zirconia (YSZ) membrane electrodes were developed with a variety of redox couples, e.g., Ni/NiO. Their potential depends on pH. When the pH value is known, these electrodes can be employed as a reference with notable applications at elevated temperatures.
Saturday, 8 March 2014
Thursday, 6 March 2014
Auxochrome
An auxochrome (Gr. Auxanein:to increase, chroma:colour) is a group of atoms attached to a chromophore which modifies the ability of that chromophore to absorb light.
They themselves fail to produce the colour; but when present along with
the chromophores in an organic compound intensifies the colour of the chromogen. Examples include the hydroxyl group (-OH), the amino group (-NH2), and an aldehyde group (-CHO).
An auxochrome is a functional group of atoms with nonbonded electrons which, when attached to a chromophore, alters both the wavelength and intensity of absorption. If these groups are in direct conjugation with the pi-system of the chromophore, they may increase the wavelength at which the light is absorbed and as a result intensify the absorption. A feature of these auxochromes is the presence of at least one lone pair of electrons which can be viewed as extending the conjugated system by resonance.
The presence of an auxochrome in the chromogen molecule is essential to make a dye. However, if an auxochrome is present in the meta position to the chromophore, it does not affect the color.
An auxochrome is known as a compound that produces a bathochromic shift, also known as red shift because it increases the wavelength of absorption, therefore moving closer to infrared light. Woodward-Fieser rules estimate the shift in wavelength of maximum absorption for several auxochromes attached to a conjugated system in an organic molecule.
An auxochrome helps a dye to bind to the object that is to be colored. Electrolytic dissociation of the auxochrome group helps in binding and it is due to this reason a basic substance takes an acidic dye.
An auxochrome is a functional group of atoms with nonbonded electrons which, when attached to a chromophore, alters both the wavelength and intensity of absorption. If these groups are in direct conjugation with the pi-system of the chromophore, they may increase the wavelength at which the light is absorbed and as a result intensify the absorption. A feature of these auxochromes is the presence of at least one lone pair of electrons which can be viewed as extending the conjugated system by resonance.
Effects on chromophore
It increases the color of any organic compound. For example, benzene does not display color as it does not have a chromophore; but nitrobenzene is pale yellow color because of the presence of a nitro group (-NO2) which acts as a chromophore. But Para-hydroxynitrobenzene exhibits a deep yellow color, in which -OH group acts as an auxochrome. Here the auxochrome (-OH) is conjugated with the chromophore -NO2. Similar behavior is seen in azobenzene which has a red color, but para-hydroxy azobenzene is dark red in color.The presence of an auxochrome in the chromogen molecule is essential to make a dye. However, if an auxochrome is present in the meta position to the chromophore, it does not affect the color.
An auxochrome is known as a compound that produces a bathochromic shift, also known as red shift because it increases the wavelength of absorption, therefore moving closer to infrared light. Woodward-Fieser rules estimate the shift in wavelength of maximum absorption for several auxochromes attached to a conjugated system in an organic molecule.
An auxochrome helps a dye to bind to the object that is to be colored. Electrolytic dissociation of the auxochrome group helps in binding and it is due to this reason a basic substance takes an acidic dye.
Explanation for the colour modification
A molecule exhibit colour because it absorbs colours only of certain frequencies and reflects or transmits others. They are capable of absorbing and emitting light of various frequencies. Light waves with frequency very close to their natural frequency are absorbed readily. This phenomenon, known as resonance, means that the molecule can absorb radiation of a particular frequency which is same as the frequency of electron movement within the molecule. Chromophore is the part of the molecule where the energy difference between two different molecular orbitals falls within the range of the visible spectrum and hence absorbs some particular colours from visible light. Hence the molecule appears coloured. When auxochromes are attached to the molecule, the natural frequency of the latter gets changed and thus the colour gets modified. Different auxochromes produce different effects in the chromophore which inturn causes absorption of light from other parts of the spectrum. Normally, auxochromes which intensifies the colour are chosen.Classification
There are mainly two types of auxochromes:- Acidic: -COOH, -OH, -SO3H
- Basic: -NHR, -NR2, -NH2
Chromophore
A chromophore is the part of a molecule responsible for its colour. The colour arises when a molecule absorbs certain wavelengths of visible light
and transmits or reflects others. The chromophore is a region in the
molecule where the energy difference between two different molecular orbitals falls within the range of the visible spectrum. Visible light that hits the chromophore can thus be absorbed by exciting an electron from its ground state into an excited state.
In biological molecules that serve to capture or detect light energy, the chromophore is the moiety that causes a conformational change of the molecule when hit by light.
In the conjugated chromophores, the electrons jump between energy levels that are extended pi orbitals, created by a series of alternating single and double bonds, often in aromatic systems. Common examples include retinal (used in the eye to detect light), various food colorings, fabric dyes (azo compounds), pH indicators, lycopene, β-carotene, and anthocyanins.
Various factors in a chromophore's structure go into determining at
what wavelength region in a spectrum the chromophore will absorb.
Lengthening or extending a conjugated system with more unsaturated (multiple) bonds in a molecule will tend to shift absorption to longer wavelengths. Woodward-Fieser rules can be used to approximate ultraviolet-visible maximum absorption wavelength in organic compounds with conjugated pi-bond systems.
Some of these are metal complex chromophores, which contain a metal in a coordination complex with ligands. Examples are chlorophyll, which is used by plants for photosynthesis and hemoglobin, the oxygen transporter in the blood of vertebrate animals. In these two examples, a metal is complexed at the center of a tetrapyrrole macrocycle ring: the metal being iron in the heme group (iron in a porphyrin ring) of hemoglobin, or magnesium complexed in a chlorin-type ring in the case of chlorophyll. The highly conjugated pi-bonding system of the macrocycle ring absorbs visible light. The nature of the central metal can also influence the absorption spectrum of the metal-macrocycle complex or properties such as excited state lifetime. The tetrapyrrole moiety in organic compounds which is not macrocyclic but still has a conjugated pi-bond system still acts as a chromophore. Examples of such compounds include bilirubin and urobilin, which exhibit a yellow color.
In a pH range of about 0-8, the molecule has three aromatic rings all bonded to a tetrahedral sp3 hybridized carbon atom
in the middle which does not make the π-bonding in the aromatic rings
conjugate. Because of their limited extent, the aromatic rings only
absorb light in the ultraviolet region, and so the compound appears
colorless in the 0-8 pH range. However as the pH increases beyond 8.2,
that central carbon becomes part of a double bond becoming sp2
hybridized and leaving a p orbital to overlap with the π-bonding in the
rings. This makes the three rings conjugate together to form an
extended chromophore absorbing longer wavelength visible light to show a
fuchsia color.At pH ranges outside 0-12, other molecular structure changes result in other color changes.
In biological molecules that serve to capture or detect light energy, the chromophore is the moiety that causes a conformational change of the molecule when hit by light.
Conjugated pi-bond system chromophores
Some of these are metal complex chromophores, which contain a metal in a coordination complex with ligands. Examples are chlorophyll, which is used by plants for photosynthesis and hemoglobin, the oxygen transporter in the blood of vertebrate animals. In these two examples, a metal is complexed at the center of a tetrapyrrole macrocycle ring: the metal being iron in the heme group (iron in a porphyrin ring) of hemoglobin, or magnesium complexed in a chlorin-type ring in the case of chlorophyll. The highly conjugated pi-bonding system of the macrocycle ring absorbs visible light. The nature of the central metal can also influence the absorption spectrum of the metal-macrocycle complex or properties such as excited state lifetime. The tetrapyrrole moiety in organic compounds which is not macrocyclic but still has a conjugated pi-bond system still acts as a chromophore. Examples of such compounds include bilirubin and urobilin, which exhibit a yellow color.
Auxochrome
An auxochrome is a functional group of atoms attached to the chromophore which modifies the ability of the chromophore to absorb light, altering the wavelength or intensity of the absorption.Halochromism in chromophores
Halochromism occurs when a substance changes color as the pH changes. This is a property of pH indicators, whose molecular structure changes upon certain changes in the surrounding pH. This change in structure affects a chromophore in the pH indicator molecule. For example, phenolphthalein is a pH indicator whose structure changes as pH changes as shown in the following table:| Structure | ||
|---|---|---|
| pH | 0−8.2 | 8.2−12.0 |
| Conditions | acidic or near-neutral | basic |
| Color name |
|
pink to fuchsia |
| Color |
Wednesday, 5 March 2014
Must watch
https://www.facebook.com/photo.php?v=439010916243683
Fight of a snake and crocodile....
who won??? Interesting.
Fight of a snake and crocodile....
who won??? Interesting.
Periodic Table
Visit this blog and at the end of the page you will find a periodic table.
Just click on any element in the table and find exact atomic number, melting and freezing point and also the weight of that element. I am sure you will find it useful.
Thanks
colourscience.blogspot.com
Just click on any element in the table and find exact atomic number, melting and freezing point and also the weight of that element. I am sure you will find it useful.
Thanks
colourscience.blogspot.com
Nernst Equation
The Nernst Equation
enables one to determine electromotive forces (emf) of many processes,
for instance the resting potential of cell membranes. We can then deduce
the biological standard potentials which are
important in studying biological process such as action potential during
a spike of a neuron in response to a stimulus.
Introduction
The Nernst Equation is derived from the emf and the Gibbs energy under non-standard conditions.
When Eo is positive, the reaction is spontaneous. When Eo is negative, the reaction is not spontaneous. Since the change in Gibbs free energy, ΔG , is also related to spontaneity of a reaction, therefore, ΔG and E are related. Specifically,
where, n is # of electrons transferred in the reaction, F is the Faraday constant (96500 C/mol) and E is potential difference. Under standard conditions, this equation is then
Since,
Substituting ΔG=−nFE and ΔGo=−nFEo into equation (1), we have:
Divide both sides of the equation above by −nF , we have
Equation (2) can be rewritten in the form of log base 10:
At standard temperature T = 298K, the 2.303RTF equals .0592 V, so equation (3) turns into:
The equation above indicates that the electrical potential of a cell depends upon the reaction quotient Q of
the reaction. As the redox reaction proceeds, reactants are consumed,
thus concentration of reactants decreases. Conversely, the products
concentration increases due to the increased in products formation. As
this happens, cell potential gradually decreases until the reaction is
at equilibrium, at which ΔG =0 .
| Example 1 |
|---|
|
For the Zn-Cu redox reaction:
Initially, [Cu2+] = [Zn2+] = 1.0 M at standard T = 298K As the reaction proceeds, [Cu2+] decreases as [Zn2+] increases. Lets say after one minute, [Cu2+] = 0.05 M while [Zn2+] = 5.0 M. According to Nernst, cell potential after 1 minute is:
As you can see, the initial cell potential is
|
At equilibrium, the reaction quotient Q=Keq . Also, at equilibrium, ΔG =0 and ΔG=−nFE , so E =0 .
Therefore, substituting Q=Keq and E =0 into the Nernst equation, we have:
At standard conditions, the equation above simplifies into:
This equation can be rearranged into:
The equation above indicates that the equilibrium constant Keq is proportional to the standard potential of the reaction. Specifically, when:
K>1,Eo>0 , reaction favors products formation.K<1,Eo<0 , reaction favors reactants formation.
This result fits Le Châtlier's Principle,which
states that when a system at equilibrium experiences a change, the
system will minimize that change by shifting the equilibrium in the
opposite direction.
Biological Application of the Nerst Equation
The
emf can be determined measuring the current in a galvanic cell. This
method is important when determining the standard potential of oxidizing
agents. But our interest is the biological standard potentials such as neurons firing.
Action Potential of a Neuron Cell
Perhaps the most fascinating system in our body is the nervous system. The neuron is the basic operating unit of the nervous system and its mechanism is still under a lot of research. Electrolytes Sodium and Potassium are the most prevalent electrolytes in our body. Intracellular concentrations of Potassium is higher inside the cell in comparison to extracellular. For Sodium
it's the opposite more extracellular and less intracellular. This
difference in concentration is the mechanics of how a neuron and other
cells have resting potentials. ATPase pumps and selective membrane
channels allow for the concentration gradient difference. With the Nernst Equation
we can deduce the membrane potential of a neuron for our discussion.
The concentration of potassium inside is 150 mM, and 15 mM outside.
Plugging these values in the equation above out comes the neuron
potential which can be depolarize in response to ...
References
- Atkins, Peter and de Paula, Julio. Physical Chemistry for the Life Sciences. New York: W.H. Freeman and Company. p. 214-222.
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