What is a disulfide in the context of chemistry?

In chemistry, a disulfide refers to a compound that contains a specific functional group with the chemical structure R−S−S−R′, or the disulfide anion, S₂²⁻. This linkage is also commonly known as an SS-bond or a disulfide bridge, and it is typically formed from two thiol groups.

What is the chemical formula for the disulfide anion?

The disulfide anion has the chemical formula S₂²⁻, which can be represented as ⁻S−S⁻. In this form, sulfur atoms have an oxidation number of -1.

How does the electron configuration of the disulfide anion's sulfur atom compare to that of chlorine?

The sulfur atom in the disulfide anion, with an oxidation number of -1, has an electron configuration that resembles that of a chlorine atom. This similarity contributes to sulfur's tendency to form covalent bonds, such as the S-S bond in the disulfide group, analogous to how chlorine exists as a diatomic molecule (Cl₂).

What is the difference between a disulfide and a persulfide?

A disulfide is characterized by the R−S−S−R′ functional group, where two sulfur atoms are bonded to organic groups. A persulfide, on the other hand, has the structure R−S−S−H, indicating that one of the sulfur atoms is bonded to a hydrogen atom.

What is the typical C-S-S-C dihedral angle found in disulfides?

Disulfides typically exhibit a C−S−S−C dihedral angle that approaches 90 degrees. This specific angle influences the molecule's overall shape and reactivity.

What is the S-S bond length in diphenyl disulfide, and how does it compare to elemental sulfur?

The S−S bond length in diphenyl disulfide is approximately 2.03 Å (angstroms). This length is similar to the S−S bond length found in elemental sulfur.

What are the two primary classifications of disulfides based on their structure?

Disulfides can be classified as either symmetrical or unsymmetrical. Symmetrical disulfides have the general formula RSSR, where both organic groups (R) attached to the sulfur atoms are identical. Unsymmetrical disulfides, also known as heterodisulfides or mixed disulfides, have the formula RSSR′, where the two organic groups are different.

Which type of disulfide is more commonly encountered in organic chemistry, and which is more prevalent in nature?

Symmetrical disulfides, with the formula RSSR, are more commonly encountered in organic chemistry. In contrast, many disulfides found in nature are unsymmetrical (heterodisulfides).

What is cystine, and what is its significance in proteins?

Cystine is an important symmetrical disulfide that is formed from two molecules of the amino acid cysteine. It acts as a crosslinker in the tertiary and quaternary structure of many proteins, contributing to their stability and shape.

How does cysteamine help in treating cystinosis?

Cysteamine is used to treat cystinosis by converting the poorly soluble cystine, which crystallizes in the disorder, into a more soluble mixed disulfide with cysteine. This process helps to remove the excess cystine from the body.

What type of chemical reaction is involved when cysteamine converts cystine?

The conversion of cystine to a mixed disulfide and cysteine by cysteamine is an example of a thiol-disulfide exchange reaction. This type of reaction involves the breaking and forming of disulfide bonds.

What is an example of a cyclic disulfide, and what is a general trend for rings with multiple disulfide bonds?

Lipoic acid, which is a 1,2-dithiolane, is a major example of a cyclic disulfide. Rings containing more than one disulfide bond tend to polymerize.

How do thiuram disulfides differ in behavior from typical organic disulfides?

Thiuram disulfides, with the formula (R₂NCSS)₂, behave distinctly from typical organic disulfides due to the presence of a thiocarbonyl group. This structural feature influences their chemical properties and reactions.

What is the bond dissociation energy of disulfide bonds?

Disulfide bonds are relatively strong, possessing a typical bond dissociation energy of 60 kcal/mol (251 kJ/mol).

How does the strength of a disulfide bond compare to carbon-carbon and carbon-hydrogen bonds?

While strong, disulfide bonds are about 40% weaker than carbon-carbon (C-C) and carbon-hydrogen (C-H) bonds. This relative weakness makes the S-S bond the 'weak link' in many molecules.

What makes the S-S bond in disulfides susceptible to scission by polar reagents?

The S-S bond in disulfides is susceptible to scission by polar reagents, both electrophiles and especially nucleophiles, due to the polarizability of divalent sulfur.

What is the general reaction that occurs when a nucleophile attacks a disulfide bond?

When a nucleophile (Nu⁻) attacks a disulfide bond (RS-SR), it leads to the formation of a new bond between the sulfur and the nucleophile (RS-Nu), releasing the other sulfur atom as a thiolate anion (RS⁻).

What is the typical length of an S-S bond in a disulfide, and how does it compare to a C-C bond?

The S-S bond in disulfides is typically around 2.05 Å long, which is about 0.5 Å longer than a C-C bond. This longer bond length contributes to its reactivity.

What is the standard reduction potential for disulfides at pH 7, and how does it compare to ferredoxins?

The standard reduction potential for disulfides at pH 7 is approximately -250 mV relative to the standard hydrogen electrode. This is significantly less negative than the standard reduction potential for ferredoxins, which is around -430 mV.

What is the general chemical equation representing the oxidation of thiols to disulfides?

The oxidation of two thiol molecules (2 RSH) to form a disulfide (RSSR) involves the release of two protons (2 H⁺) and two electrons (2 e⁻), represented by the equilibrium: 2 RSH ⇌ RSSR + 2 H⁺ + 2 e⁻.

What common laboratory reagent is used to oxidize thiols to disulfides in the presence of a base?

Iodine (I₂) in the presence of a base is commonly employed in the laboratory to oxidize thiols into disulfides.

What is thiol-disulfide exchange, and what is its significance in protein chemistry?

Thiol-disulfide exchange is a reaction where a thiolate anion (−S⁻) attacks a disulfide bond (−S−S−), displacing one sulfur atom and forming a new disulfide bond. This process is the primary mechanism for the formation and rearrangement of disulfide bonds within proteins, influencing their folding and stability.

Why is thiol-disulfide exchange inhibited at low pH?

Thiol-disulfide exchange is inhibited at low pH (typically below 8) because the thiolate anion, which is the reactive species, is protonated to form a thiol. The pKa of a typical thiol group is around 8.3, meaning at lower pH values, the equilibrium favors the less reactive thiol form.

What is disulfide shuffling, and how does it differ from oxidation/reduction?

Disulfide shuffling refers to the rearrangement of disulfide bonds within a protein, where a thiolate group attacks an existing disulfide bond, leading to a different pairing of cysteine residues. This process does not change the total number of disulfide bonds but rather their location. It is generally much faster than oxidation or reduction reactions, which alter the number of disulfide bonds.

What is the role of thioredoxin in disulfide bond metabolism in vivo?

Thioredoxin is a small protein essential in all known organisms that facilitates the *in vivo* oxidation and reduction of protein disulfide bonds through thiol-disulfide exchange. Its structure allows it to form internal disulfide bonds or bonds with other proteins, acting as a repository for reduced or oxidized disulfide moieties.

How are disulfides in proteins typically denoted?

Disulfide bonds in proteins are often denoted by hyphenating the abbreviations for the cysteine residues involved, such as 'Cys26–Cys84 disulfide bond' or more simply 'C26–C84', implying the disulfide linkage.

What is a 'disulfide species' and a 'disulfide ensemble' in the context of proteins?

A 'disulfide species' refers to a specific pairing of cysteine residues connected by a disulfide bond, often denoted like (26–84). A 'disulfide ensemble' groups together all disulfide species that have the same number of disulfide bonds, such as the 1S ensemble (one disulfide bond) or the 2S ensemble (two disulfide bonds).

How do disulfide bonds contribute to protein stability?

Disulfide bonds stabilize protein structure by holding different parts of the protein chain together, thereby biasing the protein towards a folded topology. They also destabilize the unfolded form by reducing its entropy, can form the nucleus of a hydrophobic core, and increase local residue concentration, which stabilizes secondary structures.

What is the significance of disulfide bonds in hair and feathers?

Disulfide bonds are crucial for the structural integrity of hair and feathers, which are primarily composed of keratins. The high disulfide content in these proteins contributes to their robustness, stiffness, and resistance to degradation. The manipulation of these bonds is the basis for processes like permanent waving in hairstyling.

What are some examples of inorganic disulfides?

Examples of inorganic disulfides include hydrogen disulfide (H₂S₂), disulfur dichloride (S₂Cl₂), and iron disulfide (FeS₂), also known as pyrite.

Why is carbon disulfide (CS₂) not considered a disulfide in the typical sense?

Carbon disulfide (CS₂), with its structure S=C=S, is not considered a disulfide in the typical sense because it lacks the characteristic S-S single bond. Instead, it features a carbon atom double-bonded to two sulfur atoms.

What is the role of disulfide bonds in the vulcanization of rubber?

In the vulcanization of rubber, disulfide and polysulfide bonds act as crosslinking agents. These S-S linkages significantly affect the material's stability and rheology, with a greater degree of crosslinking leading to a stronger and more rigid rubber.

What is the typical pKa of a thiol group, and why is it relevant to thiol-disulfide exchange?

The pKa of a typical thiol group is approximately 8.3. This value is relevant because thiol-disulfide exchange requires the thiolate anion (S⁻), which is the deprotonated form of the thiol. At pH values below the pKa, the thiol is predominantly protonated, making the exchange reaction less favorable.

What are the general conditions under which stable disulfide bonds are formed in eukaryotic cells?

In eukaryotic cells, stable disulfide bonds are generally formed in the lumen of the rough endoplasmic reticulum (RER) and the mitochondrial intermembrane space. These compartments have a more oxidizing environment compared to the cytosol, which is typically a reducing environment.

What types of proteins in eukaryotes typically contain disulfide bonds?

Disulfide bonds are most commonly found in proteins that are secreted to the extracellular medium, lysosomal proteins, and the exoplasmic domains of membrane proteins, due to the oxidizing conditions in these cellular locations.

What is the function of disulfide bonds in bacteria when exposed to oxidative stress?

In bacteria, disulfide bonds serve as a protective, reversible switch that can turn proteins on or off. They help protect cellular components, such as DNA, from damage caused by oxidative reactions like those involving hydrogen peroxide (H₂O₂).

What are some exceptions to the rule that disulfide bonds are not found in the cytosol of eukaryotic cells?

Exceptions include disulfide crosslinking of nuclear and cytosolic proteins during necrotic cell death, and the presence of disulfide bonds in some cytosolic proteins that function as oxidation sensors or redox catalysts. Additionally, the virus Vaccinia produces cytosolic proteins with many disulfide bonds, though the reason is not fully understood.

How do disulfide bonds in regulatory proteins function as a signaling element?

Because disulfide bonds can be reversibly reduced and re-oxidized, their redox state has evolved to act as a signaling mechanism. For instance, in chloroplasts, the reduction of disulfide bonds by the ferredoxin-thioredoxin system is linked to the control of metabolic pathways and gene expression, adjusting cellular activity based on light intensity.

What is the chemical formula for disulfur dichloride, and what is its industrial significance?

Disulfur dichloride has the chemical formula S₂Cl₂ and is described as a common industrial chemical. It is a liquid that can be distilled.

What is the chemical formula for pyrite, and what is its common name?

Pyrite, also known as "fool's gold," is an iron disulfide with the chemical formula FeS₂. Its structure involves iron atoms and disulfide anions.

What is the general reaction for the reduction of disulfides to thiols using hydride agents?

Hydride agents, such as sodium borohydride, can reduce disulfides (RSSR) to thiols (RSH). The reaction can be represented as: RSSR + 2 Na → 2 NaSR, followed by protonation of the resulting sodium thiolate (NaSR + HCl → HSR + NaCl).

What are the products of the oxidation of disulfides with halogens, such as chlorine?

When disulfides (like ArSSAr) are oxidized with halogens, such as chlorine (Cl₂), they form sulfenyl halides (ArSCl). The reaction is: ArSSAr + Cl₂ → 2 ArSCl.

What are the sequential oxidation products of disulfides?

Further oxidation of disulfides (RSSR) first yields thiosulfinates (RS(=O)SR), and subsequent oxidation produces thiosulfonates (RS(=O)₂SR).

What is the role of tris(2-carboxyethyl)phosphine (TCEP) in protein thiol modification?

Tris(2-carboxyethyl)phosphine (TCEP) is a reductant used in protein thiol modification. It is advantageous because it is odorless, selective, works under both alkaline and acidic conditions, is more hydrophilic, more resistant to oxidation, and often does not need to be removed before modifying protein thiols.

What is the typical S-S bond length in a disulfide, and how does it compare to a C-C bond?

The S-S bond length in a disulfide is approximately 2.05 Å, which is about 0.5 Å longer than a typical C-C bond. This difference in length can contribute to the reactivity of the S-S bond.

What is the significance of the disulfide bond in the context of protein folding and stability?

Disulfide bonds are crucial for the folding and stability of many proteins, particularly those secreted outside the cell. They act as covalent cross-links that hold different parts of the protein chain together, thereby reducing the conformational entropy of the unfolded state and stabilizing the folded structure.

What is the chemical structure of the disulfide functional group?

The disulfide functional group has the chemical structure R−S−S−R′, where 'R' and 'R′' represent organic groups attached to the two sulfur atoms that are bonded to each other.

What is the difference between a disulfide and a thiosulfoxide?

Thiosulfoxides are isomers of disulfides but differ in their structure. While disulfides have a continuous chain of two sulfur atoms (S-S), thiosulfoxides have the second sulfur atom branching from the first, represented as >S=S rather than -S-S-.

What are compounds with three sulfur atoms called?

Compounds containing three sulfur atoms in a chain, such as CH₃S−S−SCH₃, are referred to as trisulfides.

What is the role of disulfide bonds in the sperm chromatin of mammals?

In many mammalian species, disulfide bonds are formed within and between protamines found in sperm chromatin. These bonds contribute to the structural organization and stability of the genetic material within sperm cells.

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Introduction

The Disulfide Functional Group

In chemistry, a disulfide (or disulphide in British English) refers to a compound featuring the R−S−S−R′ functional group. This linkage, often termed an SS-bond or disulfide bridge, is typically derived from two thiol groups. The corresponding anion is S₂²⁻.

Significance Across Disciplines

While the disulfide anion appears in rare inorganic minerals, the functional group itself holds immense importance in biochemistry. Specifically, disulfide bridges formed between cysteine residues are critical determinants of protein tertiary and quaternary structure. The term "disulfide" originates from the Greek word "karkinos" (crab), reflecting early observations of tumorous growths.

Distinction from Bisulfides

It is important to distinguish disulfides from bisulfides. Bisulfides, such as the bisulfide anion (HS⁻) or compounds containing the −SH group (thiols), represent a different chemical entity and reactivity profile.

Molecular Structure

C-S-S-C Geometry

Disulfide compounds exhibit a C−S−S−C dihedral angle that typically approaches 90 degrees. The S−S bond length, observed to be approximately 2.03 Å in diphenyl disulfide, is comparable to that found in elemental sulfur. This specific geometry influences the molecule's reactivity and stability.

Symmetric vs. Asymmetric

Disulfides can be classified as symmetric (RSSR) or asymmetric (RSSR′, also known as heterodisulfides or mixed disulfides). While symmetric disulfides are more common in general organosulfur chemistry, many biologically relevant disulfides are asymmetric. The conversion of symmetric cystine to more soluble mixed disulfides, as seen in cystinosis treatment, exemplifies the importance of this distinction.

Chemical Properties

Bond Strength and Reactivity

The disulfide bond possesses a significant bond dissociation energy, approximately 60 kcal/mol (251 kJ/mol). However, being about 40% weaker than C−C and C−H bonds, it often represents the weakest link in a molecule. The S−S bond is susceptible to cleavage by polar reagents, particularly nucleophiles (Nu⁻), following the general reaction: RS−SR + Nu⁻ → RS−Nu + RS⁻.

Redox Potential and Dihedral Angles

Disulfides exhibit a preference for dihedral angles approaching 90°. When this angle deviates towards 0° or 180°, the disulfide acts as a more potent oxidant. The equilibrium constant for the reduction of disulfides to thiols provides a measure of their standard redox potential, typically around −250 mV versus the standard hydrogen electrode at pH 7.

Synthesis Pathways

Oxidation of Thiols

Disulfide bonds are predominantly formed through the oxidation of thiol (−SH) groups. This process can be facilitated by various oxidants, including molecular oxygen and hydrogen peroxide. In laboratory settings, iodine in the presence of a base is a common reagent for this transformation. Metal complexes, such as copper(II) and iron(III), also catalyze this reaction.

Unsymmetrical Disulfide Formation

Specialized methods are employed for the synthesis of unsymmetrical disulfides. Reagents that deliver the equivalent of "RS⁺" react with thiols to yield these mixed disulfides. Bunte salts (RSSO₃Na) are also utilized, reacting with thiols to form unsymmetrical disulfides and sodium sulfite. These methods are crucial for creating specific molecular architectures.

Key Chemical Reactions

Cleavage and Reduction

The cleavage of the disulfide bond is a fundamental reaction. Various reductants convert disulfides back to thiols. Common laboratory reagents include sodium borohydride and dithiothreitol (DTT). Alkali metals also effect this reduction, typically followed by protonation of the resulting thiolate. Tris(2-carboxyethyl)phosphine (TCEP) is noted for its selectivity and stability.

Thiol-Disulfide Exchange

A critical reaction in biological systems is thiol-disulfide exchange. Here, a thiolate anion attacks a disulfide bond, leading to the formation of a new disulfide and releasing a thiolate. This process is pH-dependent, favoring the thiolate form at pH > 8. It is central to protein folding, rearrangement (disulfide shuffling), and redox regulation, often mediated by enzymes like thioredoxin.

Biological Significance

Protein Structure and Stability

Disulfide bonds are vital for the oxidative folding and stability of many proteins, particularly those secreted into the oxidizing extracellular environment. They stabilize protein conformation by holding polypeptide segments together, effectively lowering the entropy of the unfolded state and contributing to the hydrophobic core. Exceptions exist, with some cytosolic proteins utilizing disulfides for redox sensing.

Cellular Protection

In bacteria, disulfide bonds offer protection against oxidative stress, such as from hydrogen peroxide, safeguarding DNA and cellular integrity. Archaea generally exhibit fewer disulfides compared to higher organisms. In eukaryotes, stable disulfide formation primarily occurs in the rough endoplasmic reticulum (RER) and mitochondrial intermembrane space, environments conducive to oxidation.

Regulatory Roles

The reversible nature of disulfide bonds allows them to function as redox switches in regulatory proteins. In chloroplasts, the ferredoxin-thioredoxin system utilizes disulfide reduction to modulate metabolic pathways and gene expression in response to light intensity. Certain bacterial two-component systems also employ redox-sensitive cystine disulfide bonds for regulatory control.

Structural Components

Disulfide bonds are abundant in structural proteins like keratins found in hair and feathers, contributing significantly to their robustness and resistance. The manipulation of these bonds is the basis for hairstyling techniques such as permanent waving. The high sulfur content from disulfides also contributes to the characteristic odor of burning hair or feathers.

Disease Implications

Disruptions in disulfide metabolism can lead to disease. Cystinosis, characterized by the precipitation of cystine in organs, is a condition where the solubility of disulfide is compromised. Treatment with cysteamine aims to solubilize cystine by forming more soluble mixed disulfides and reducing it to cysteine.

Inorganic Disulfides

The Disulfide Anion

The inorganic disulfide anion is S₂²⁻, where sulfur exists in the −1 oxidation state. This configuration is analogous to elemental chlorine (Cl₂), with each sulfur atom resembling a chlorine atom in its electron configuration. This similarity drives the formation of the S−S covalent bond.

Examples in Minerals

Notable inorganic disulfides include hydrogen disulfide (H₂S₂), the simplest example. Disulfur dichloride (S₂Cl₂) is a common industrial chemical. In mineralogy, iron disulfide (FeS₂), known as pyrite or "fool's gold," is a prominent example, showcasing the stability of the disulfide anion within crystal lattices.

Industrial Applications

Rubber Vulcanization

Beyond their biological roles, disulfides are integral to the vulcanization of rubber. This process involves crosslinking polymer chains with sulfur, forming disulfide (and polysulfide) bonds. These linkages significantly enhance the material's stability, rigidity, and rheological properties. The extent of crosslinking directly correlates with the material's strength, classifying rubber as a thermoset material due to the irreversible nature of these bonds.

Nomenclature and Related Groups

Distinguishing Disulfides

It is crucial to differentiate true disulfides (containing an S−S bond) from compounds with similar names but different structures. Carbon disulfide (CS₂) and molybdenum disulfide (MoS₂) do not possess an S−S bond and are thus not disulfides in the conventional sense. Thiosulfoxides (>S=S) are isomers of disulfides, differing in the arrangement of the sulfur atoms.

Analogous Bonds

Disulfide bonds share analogies with related linkages such as peroxide (−O−O−), thioselenide (−S−Se−), and diselenide (−Se−Se−) bonds. Intermediate compounds, like thioperoxides (R¹OSR²), are isomeric to sulfoxides, paralleling the relationship between disulfides and thiosulfoxides.

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References

TCEP technical information, from Interchim

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The Sulfur-Sulfur Link

💡 Dive in with Flashcard Learning! 💡

Introduction ℹ️

🔗 The Disulfide Functional Group

🔬 Significance Across Disciplines

⚠️ Distinction from Bisulfides

Molecular Structure 🔗

📐 C-S-S-C Geometry

⚖️ Symmetric vs. Asymmetric

Chemical Properties 🧪

⚡ Bond Strength and Reactivity

🔄 Redox Potential and Dihedral Angles

Synthesis Pathways 🛠️

💧 Oxidation of Thiols

✨ Unsymmetrical Disulfide Formation

Key Chemical Reactions ⚛️

✂️ Cleavage and Reduction

🔄 Thiol-Disulfide Exchange

Biological Significance 🧬

🧬 Protein Structure and Stability

🛡️ Cellular Protection

🌿 Regulatory Roles

💇 Structural Components

💔 Disease Implications

Inorganic Disulfides ⛏️

⚛️ The Disulfide Anion

💎 Examples in Minerals

Industrial Applications 🏭

🚗 Rubber Vulcanization

Nomenclature and Related Groups 🏷️

🤔 Distinguishing Disulfides

🧪 Analogous Bonds

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📜 Important Notice

Dive in with Flashcard Learning!

Introduction

The Disulfide Functional Group

Significance Across Disciplines

Distinction from Bisulfides

Molecular Structure

C-S-S-C Geometry

Symmetric vs. Asymmetric

Chemical Properties

Bond Strength and Reactivity

Redox Potential and Dihedral Angles

Synthesis Pathways

Oxidation of Thiols

Unsymmetrical Disulfide Formation

Key Chemical Reactions

Cleavage and Reduction

Thiol-Disulfide Exchange

Biological Significance

Protein Structure and Stability

Cellular Protection

Regulatory Roles

Structural Components

Disease Implications

Inorganic Disulfides

The Disulfide Anion

Examples in Minerals

Industrial Applications

Rubber Vulcanization

Nomenclature and Related Groups

Distinguishing Disulfides

Analogous Bonds

Teacher's Corner

True or False?

Test Your Knowledge!

Gamer's Corner

Discover other topics to study!

References

Feedback & Support

Disclaimer

Important Notice