Metabolic Pathways and ATP Regulation

<p>All of the above (D)</p> Signup and view all the answers

<p>To receive electrons from CoQH2 and pass them to Complex IV (C)</p> Signup and view all the answers

<p>Complex II (D)</p> Signup and view all the answers

<p>CoQH2 is a two-electron donor, transferring electrons to one-electron acceptors. (B)</p> Signup and view all the answers

<p>FAD receives electrons from succinate and transfers them to CoQ. (B)</p> Signup and view all the answers

<p>It involves a series of proteins that receive high energy electrons from NAD+ and FADH2. (B)</p> Signup and view all the answers

<p>Inner mitochondrial membrane (A)</p> Signup and view all the answers

<p>ATP synthase (B)</p> Signup and view all the answers

<p>It acts as a mobile carrier for electrons between Complex I and Complex III. (D)</p> Signup and view all the answers

<p>Oxygen (B)</p> Signup and view all the answers

<p>Glucose (D)</p> Signup and view all the answers

<p>To provide the energy for ATP synthase to produce ATP. (B)</p> Signup and view all the answers

<p>NADH and FADH2 (B)</p> Signup and view all the answers

<p>Complex V (D)</p> Signup and view all the answers

<p>It provides a compartmentalized space for the electron transport chain. (A)</p> Signup and view all the answers

<p>The presence of a high-energy phosphate bond, readily hydrolyzed. (B)</p> Signup and view all the answers

<p>The phosphoanhydride bonds in ATP are responsible for its high-energy character. (A)</p> Signup and view all the answers

<p>It ensures that ATP's energy is released only when needed, preventing spontaneous hydrolysis. (B)</p> Signup and view all the answers

<p>These variations are critical for maintaining the appropriate function of different organelles. (A)</p> Signup and view all the answers

<p>They are responsible for the release of free energy, powering cellular processes. (B)</p> Signup and view all the answers

<p>F0/F1 or Complex V (ATP Synthase) (C)</p> Signup and view all the answers

<p>2.5 moles (D)</p> Signup and view all the answers

<p>They transfer electrons from cytochrome c to oxygen. (B)</p> Signup and view all the answers

<p>It remains latent until a complex facilitates proton re-entry. (B)</p> Signup and view all the answers

<p>Inner mitochondrial matrix (B)</p> Signup and view all the answers

<p>Iron (C), Copper (A)</p> Signup and view all the answers

<p>To form ATP from ADP and inorganic phosphate using the proton gradient. (C)</p> Signup and view all the answers

<p>Both A and C (B)</p> Signup and view all the answers

<p>X-ray diffraction (A)</p> Signup and view all the answers

<p>Pepsin (C)</p> Signup and view all the answers

<p>The bond between Arginine (15) and Isoleucine (16) (B)</p> Signup and view all the answers

<p>Chymotrypsin hydrolyzes peptide bonds adjacent to aromatic amino acids. (A)</p> Signup and view all the answers

<p>Reversible phosphorylation of the zymogen. (C)</p> Signup and view all the answers

<p>To prevent self-digestion of the pancreas. (A)</p> Signup and view all the answers

<p>Absorbing the smaller peptides and amino acids produced by protein digestion. (A)</p> Signup and view all the answers

<p>Trypsinogen is activated by a specific protease called enteropeptidase. (D)</p> Signup and view all the answers

<p>They promote the cooperative binding of oxygen to hemoglobin. (C)</p> Signup and view all the answers

<p>Serine (Ser), Threonine (Thr), Tyrosine (Tyr) (D)</p> Signup and view all the answers

<p>To remove a phosphate group from an enzyme, deactivating it. (D)</p> Signup and view all the answers

<p>The binding affinity of the protein for the substrate remains constant across all substrate concentrations. (A)</p> Signup and view all the answers

<p>The curve shifts to the right, indicating a decrease in oxygen affinity. (A)</p> Signup and view all the answers

<p>All of the above (D)</p> Signup and view all the answers

<p>ATP provides energy for the kinase to catalyze the phosphorylation reaction. (C)</p> Signup and view all the answers

<p>Phosphorylation can either activate or inactivate the enzyme, depending on the specific enzyme. (C)</p> Signup and view all the answers

<p>To catalyze the addition of a phosphate group to a protein. (A)</p> Signup and view all the answers

<p>ATP provides a phosphate group for the phosphorylation reaction. (D)</p> Signup and view all the answers

<p>The enzyme might be constitutively inactive, even in the presence of an activating signal. (B)</p> Signup and view all the answers

<p>The T state has a lower affinity for oxygen, while the R state has a higher affinity for oxygen. (D)</p> Signup and view all the answers

<p>The subunits interact with each other, influencing the binding affinity of other subunits for the substrate. (A)</p> Signup and view all the answers

<p>Homoallostery involves interactions between identical subunits, while heteroallostery involves interactions between different subunits. (C)</p> Signup and view all the answers

<p>The protein exhibits a sigmoidal binding curve, showing a gradual increase followed by a sharp increase in binding. (C)</p> Signup and view all the answers

<p>Ribose moieties are added to the ADP residue of a protein. (C)</p> Signup and view all the answers

<p>To remove phosphate groups from proteins. (A)</p> Signup and view all the answers

Energy that remains latent until utilized by a process.

A protein that transfers electrons to oxygen in cellular respiration.

Complexes that facilitate electron transfer from cytochrome C to oxygen.

An enzyme that re-enters protons into the mitochondrial matrix, generating ATP.

NADH produces approximately 2.5 moles of ATP during respiration.

A difference in proton concentration across a membrane, driving ATP synthesis.

The space within the inner membrane of mitochondria, where key processes occur.

A measure of how many moles of ATP can be generated from electron carriers like NADH.

The differences in ion concentrations across organelle membranes, often by several orders of magnitude.

Molecules that assist enzymes in catalyzing reactions, often by donating or accepting chemical groups.

Chemical bonds in compounds like ATP that release significant energy when broken, e.g., -25 kJ/mol.

ATP has high-energy character due to its stable bonds that release large amounts of free energy upon hydrolysis.

Reactions where a phosphate group is transferred, crucial for energy transfer in biological systems.

Inactive enzyme precursors synthesized by the pancreas.

The irreversible process of converting zymogens to active enzymes.

An active proteolytic enzyme activated from chymotrypsinogen.

Activation process where an enzyme activates itself and others.

The inactive form of trypsin, an essential digestive enzyme.

Technique to analyze protein structures through X-ray diffraction.

The precise cutting of a protein at specific amino acid sites.

An enzyme secreted by the stomach that starts protein digestion.

A cofactor that receives electrons from NADH and transfers them to Fe-S clusters.

Cofactors within Complex I that accept electrons from FMN, transferring them onward.

A mobile electron transporter that takes electrons from Fe-S clusters and transfers them.

Complex that catalyzes the transfer of electrons from CoQH2 to cytochrome c.

Enzyme that extracts electrons from succinate using FAD as a coenzyme.

A coenzyme that donates electrons during the oxidation of succinate in Complex II.

A process where NADH is converted to NAD+, allowing electron flow into the transport chain.

Double membranous organelle consisting of an outer and inner membrane.

The outer layer of mitochondria that separates it from the cytoplasm.

The inner layer tightly folded into cristae, housing protein complexes.

Folded invaginations of the inner membrane that increase surface area for reactions.

A series of protein complexes that transfer electrons from NADH and FADH2.

The process of producing ATP, fueled by electrons from the chain.

First protein complex in the chain, acts as a proton pump.

Process of ATP formation linked to the transfer of electrons to O2.

The state of hemoglobin with lower affinity for oxygen.

The state of hemoglobin with higher affinity for oxygen.

Substances that drive proteins toward the T state, reducing their function.

The enhanced affinity of subunits for a substrate due to the binding of another subunit.

Regulation where the binding of a ligand to one subunit influences others in identical subunits.

The addition of a phosphate group to proteins that alters their function.

An enzyme that adds phosphate groups to other molecules.

An enzyme that removes phosphate groups from molecules.

A chemical change in proteins affecting their function through various additions.

Addition of ribose moieties to a protein affecting its function.

Addition of acetyl groups that can alter gene expression.

Graph shape indicating cooperative binding behavior in enzymes.

Graph shape indicating non-cooperative binding behavior.

A structural change in a protein due to post-translational modification.

Forces between charged amino acids that can influence protein structure.