Answer :
Final answer:
The question concerns the hybridization of a carbon atom in an enzyme-catalyzed reaction, specifically the carbon to which the oxygen atom of Serine 195 is bound. sp hybridization results in a linear geometry, sp² in trigonal planar, and sp³ in tetrahedral. Correctly identifying the hybridization allows us to determine which atom the oxygen of Ser 195 is bound to.
Explanation:
The interaction between Ser 195 and the intermediate is a key aspect of understanding the mechanism of an enzymatic reaction. Specifically, we must identify the type of hybridization of the carbon atom to which the oxygen of Ser 195 is bound. Given the nature of the hybridized orbitals and the molecular geometry they create, we can determine which statement is correct.
sp hybridization
In sp hybridization, a carbon atom has two sp-hybridized orbitals, which form sigma bonds at a 180° angle, creating a linear geometry. This hybridization is associated with carbon atoms in triple bonds or cumulated double bonds as in acetylene (ethyne, HC≡CH). There would be two pi bonds perpendicular to the linear arrangement formed by unhybridized p-orbitals.
sp² hybridization
For sp² hybridization, three hybridized orbitals form sigma bonds in a trigonal planar geometry. This hybridization occurs in carbons with one double bond or with resonance structures having delocalized pi bonds.
sp³ hybridization
Carbon atoms with sp³ hybridization have four single bonds, resulting in a tetrahedral geometry. This is the most common hybridization for carbons with only single bonds.
Therefore, the correct statement would involve the proper hybridization based on the described geometry around the carbon atom in the intermediate. If Ser 195's oxygen is bound to an sp² hybridized carbon, it can be part of a double bond, while an sp hybridized carbon would be in a triple bond or linear structure.
The statement that is consistent with the interaction between Ser 195 and the intermediate is that Atom OG of Ser 195 is covalently bound to atom CB of GBS, which is an sp hybridized carbon.
The answer is B. The enzyme Serine protease catalyzes the hydrolysis of peptide bonds. The active site of the enzyme has a catalytic triad composed of aspartic acid, histidine, and serine. During hydrolysis, the hydroxyl group on the serine residue nucleophilically attacks the carbonyl group of the substrate's peptide bond.
A covalent bond is formed between the Serine hydroxyl and the carbonyl carbon, resulting in an intermediate. A tetrahedral intermediate is created when the carbonyl oxygen of the substrate and the hydroxyl group of Serine are attached.
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