Exam 2 Flashcards
(142 cards)
A reactant species that is electron rich and attacks another reactant deficient in electrons is termed an electrophile.
False.
When a carbon-carbon bond is split such that one carbon atom loses both electrons, that carbon atom becomes a carbocation.
True.
A transition state proposed to form as part of a reaction mechanism is a transient species that cannot be trapped and studied.
True.
The interior of a globular protein is generally a hydrophobic region. The active site of an enzyme is usually a cleft or pit in the globular protein. All the amino acid residues in the active site, therefore, have hydrophobic side chains.
False.
Ping-pong kinetics are a hallmark of enzymes that catalyze reactions involving covalent catalysis.
True.
Relatively strong binding of reactants in the enzyme active site is necessary for efficient catalysis.
False.
Entropy of reactants increases as reactants are bound by enzymes.
False.
An enzyme active site binds more tightly to a transition-state analog than to its substrate.
True.
Chymotrypsin is a proteolytic enzyme with three alpha-amino termini (N-termini).
True.
Serine proteases contain the same amino acid residues in the catalytic triad that are part of their active sites.
True.
Enzymes typically have an optimal pH range that is based on the protonation state of ionizable groups within the active site.
True.
A free radical is a transient species that results from C-C bond cleavage that leaves a C with an unpaired electron.
True.
A/an ______________ is the species formed when bond cleavage leaves a carbon with both electrons.
carbanion
The ____________ is a description of the bond-breaking and bond-forming events in a chemical reaction.
mechanism
The ________________ is the term for a highly energetic chemical species in which bonds are being formed and broken prior to product formation in an enzyme-catalyzed reaction.
transition state
The energy required for reactants to reach the transition state from their group state is called the ___________ of the reaction.
Ea
In a ______________ reaction, every collision between reactant molecules gives rise to product.
diffusion controlled
Rate enhancement by the binding of reactants close to each other in the enzyme active site is called the _______________.
proximity effect
For a substrate with a positive charge, _______________ or _________________ might be present near the binding site on an enzyme to aid in substrate binding.
aspartate
glutamate
Very strong hydrogen bonds that form when the electronegative atoms are less than 0.25 nm apart are termed _____________________.
low barrier hydrogen bonds
In the catalytic triad of serine proteases, the side chain of a __________ residue acts as a covalent catalyst.
serine
___________________ is the term applied to the catalytic mode that involves increased binding of transition states to enzymes as compared with binding of substrates or products.
Transition state stabilization
The four major modes of enzymic catalysis are ____________, _____________, ____________, and___________.
acid-base catalysis
proximity effects
covalent catalysis
transition state stabilization
Activation of an enzyme by a substrate-initiated conformation change is called ______________.
induced fit