Biochemistry ATP and Heme Synthesis Quiz

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Questions and Answers

What initiates the formation of ATP during the proton flow through ATP synthase?

  • The release of inorganic phosphate from the F₁ component
  • The conversion of pyruvate to glucose
  • The influx of protons leading to mechanical rotation of the c-ring (correct)
  • The direct binding of ADP to the F₁ component

Which of the following statements about glycolysis is accurate?

  • Glycolysis exclusively occurs in the mitochondria of cells.
  • Glycolysis requires oxygen to generate ATP.
  • Glycolysis is an anabolic process that synthesizes glucose from ADP.
  • Glycolysis converts glucose into pyruvate, producing ATP in the process. (correct)

Which component of ATP synthase directly converts the mechanical energy from proton flow into chemical energy?

  • F₁ component (correct)
  • Proton gradient
  • c-ring
  • F₀ component

What is the primary purpose of gluconeogenesis in carbohydrate metabolism?

<p>To synthesize glucose from non-carbohydrate sources (B)</p> Signup and view all the answers

What role does the electrochemical potential play in proton flow through ATP synthase?

<p>It drives the influx of protons into the matrix. (B)</p> Signup and view all the answers

Which enzyme in the heme synthesis pathway is primarily regulated by negative feedback inhibition from heme levels?

<p>Aminolevulinic Acid Synthase (ALAS) (A)</p> Signup and view all the answers

How does low iron availability affect the activity of Aminolevulinic Acid Synthase (ALAS)?

<p>It enhances ALAS activity to promote ALA production. (D)</p> Signup and view all the answers

Which factor directly inhibits the activity of Aminolevulinic Acid Dehydratase (ALAD)?

<p>Lead (Pb2+) (A)</p> Signup and view all the answers

What determines the activity of Uroporphyrinogen Decarboxylase in the heme synthesis pathway?

<p>Availability of uroporphyrinogen III (C)</p> Signup and view all the answers

Which of the following statements regarding ferrochelatase's regulation is true?

<p>It is regulated by the availability of iron for incorporation into protoporphyrin IX. (D)</p> Signup and view all the answers

What is the primary purpose of substrate-level phosphorylation in metabolism?

<p>To generate ATP directly (D)</p> Signup and view all the answers

Which statement accurately describes the role of NADH and FADH₂ in the electron transport chain?

<p>They donate electrons to the electron transport chain, enabling ATP synthesis (D)</p> Signup and view all the answers

How do feedback mechanisms regulate metabolism?

<p>By maintaining cellular energy levels in response to ATP and ADP concentrations (D)</p> Signup and view all the answers

What is the significance of chemiosmosis in oxidative phosphorylation?

<p>It uses the established proton gradient to synthesize ATP (B)</p> Signup and view all the answers

What is the primary way that oxidative phosphorylation contributes to ATP production?

<p>By establishing a proton gradient that drives ATP synthesis (D)</p> Signup and view all the answers

Which of the following best describes anaplerotic reactions?

<p>Reactions that replenish intermediates in metabolic cycles (C)</p> Signup and view all the answers

Where does the electron transport chain primarily take place?

<p>On the inner mitochondrial membrane (B)</p> Signup and view all the answers

How does the body remove metabolic waste produced during respiration?

<p>Through CO₂ production, maintaining acid-base balance (A)</p> Signup and view all the answers

What does the term 'gluconeogenesis' specifically refer to?

<p>Synthesis of glucose from non-carbohydrate sources (B)</p> Signup and view all the answers

Which of the following describes the primary importance of gluconeogenesis?

<p>Supply of glucose to vital organs during fasting (A)</p> Signup and view all the answers

Which molecule is primarily produced during oxidative deamination?

<p>Alpha-ketoglutarate (A)</p> Signup and view all the answers

Which coenzyme is crucial for the process of transamination?

<p>Pyridoxal phosphate (PLP) (A)</p> Signup and view all the answers

What is the fate of nitrogen from amino acids in the body?

<p>Converted to urea for excretion (A)</p> Signup and view all the answers

In which part of the cell does the urea cycle initially occur?

<p>Mitochondria (A)</p> Signup and view all the answers

Which substance serves as a temporary storage of amino groups during transamination?

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

What is the primary source of carbon atoms in the synthesis of urea?

<p>Carbon dioxide (CO2) (D)</p> Signup and view all the answers

What is produced from pyruvate during the gluconeogenesis process?

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

Which enzyme is primarily responsible for the removal of amino groups during oxidative deamination?

<p>Glutamate dehydrogenase (A)</p> Signup and view all the answers

Which hormone is responsible for stimulating beta-oxidation during periods of fasting?

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

What effect does high ATP levels have on beta-oxidation?

<p>Inhibits oxidation (A)</p> Signup and view all the answers

Which statement correctly describes the role of malonyl-CoA in the regulation of beta-oxidation?

<p>It inhibits CPT I, thereby regulating fatty acid entry into mitochondria. (D)</p> Signup and view all the answers

During which state is beta-oxidation downregulated and carbohydrate metabolism favored?

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

What is the primary function of ketone bodies when glucose is scarce?

<p>To act as an alternative energy source for tissues, particularly the brain (C)</p> Signup and view all the answers

Which of the following is NOT a type of ketone body?

<p>Acetyl-CoA (A)</p> Signup and view all the answers

What is the main regulatory enzyme in the process of ketogenesis?

<p>HMG-CoA Synthase (B)</p> Signup and view all the answers

What promotes ketone body production during periods of low carbohydrate availability?

<p>Elevated free fatty acid concentrations (C)</p> Signup and view all the answers

Which statement accurately describes the relationship between hemoglobin structure and function?

<p>The quaternary structure enhances hemoglobin's ability to transport oxygen efficiently. (A)</p> Signup and view all the answers

In which way does hemoglobin contribute to pH regulation in the blood?

<p>By binding to protons (H⁺ ions) to buffer changes in acidity. (D)</p> Signup and view all the answers

What role does cooperative binding play in oxygen transport by hemoglobin?

<p>It increases the overall affinity for oxygen as more oxygen binds. (C)</p> Signup and view all the answers

Which of the following statements about the heme group's iron atom is correct?

<p>The iron atom is essential for reversible binding of oxygen. (B)</p> Signup and view all the answers

What is the primary function of hemoglobin in relation to carbon dioxide?

<p>It transports only a small percentage of carbon dioxide from tissues to lungs. (C)</p> Signup and view all the answers

Which chain types are primarily found in adult hemoglobin?

<p>Two alpha and two beta chains. (B)</p> Signup and view all the answers

Where does the binding of oxygen to hemoglobin primarily occur?

<p>In the lungs where oxygen is inhaled. (C)</p> Signup and view all the answers

What is the maximum number of oxygen molecules that one hemoglobin molecule can bind?

<p>Four oxygen molecules. (A)</p> Signup and view all the answers

Flashcards

What is oxidative phosphorylation?

The process of generating ATP by transferring electrons in the electron transport chain (ETC) and creating a proton gradient.

What is the 'oxidative' part?

The oxidation reactions that occur in the electron transport chain (ETC).

What is the 'phosphorylation' part?

The addition of a phosphate group (Pi) to ADP to form ATP.

Where does oxidative phosphorylation occur?

The inner membrane of the mitochondria.

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What is the electron transport chain (ETC)?

A series of protein complexes (I-IV) and mobile carriers (Coenzyme Q and cytochrome c) that transfer electrons from NADH and FADH₂ to oxygen.

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How does the ETC create a proton gradient?

Energy released by electron movement is used to pump protons from the mitochondrial matrix into the intermembrane space.

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What is chemiosmosis?

Utilizing the proton gradient to synthesize ATP. ATP synthase catalyzes this process.

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What's the function of oxidative phosphorylation?

It produces ATP, the energy currency of the cell, crucial for cellular functions.

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Glycolysis

The breakdown of glucose to pyruvate, producing ATP and setting the stage for complete oxidation of glucose.

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Gluconeogenesis

The process of creating glucose from non-carbohydrate sources like pyruvate or amino acids.

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Cellular Respiration

A series of metabolic reactions that occur in all living cells to extract energy from glucose.

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Catabolic Process

The process of breaking down organic molecules to release energy, typically in the form of ATP, for cellular processes.

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Anabolic Process

The process of building up complex molecules from simpler ones, requiring energy, typically in the form of ATP.

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Pyruvate to Glucose Conversion

The conversion of pyruvate to glucose, a key step in gluconeogenesis.

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Production of Acetyl-CoA

A metabolic pathway that generates acetyl-CoA from glucose, fatty acids, and amino acids.

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β-oxidation

The breakdown of fatty acids into acetyl-CoA, a process that releases energy.

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Transamination

The removal of amino groups from amino acids and their transfer to keto acids. This process is catalyzed by aminotransferases.

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Oxidative Deamination

The process of removing ammonia (NH4+) from glutamate, catalyzed by glutamate dehydrogenase.

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Urea Cycle

A cycle that occurs in the liver, converting ammonia into urea for excretion.

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Oxidative Phosphorylation

The process of producing ATP from the energy stored in NADH and FADH2, which are generated in the TCA cycle.

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TCA Cycle

A series of reactions that break down acetyl-CoA to carbon dioxide, generating NADH and FADH2.

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Beta-oxidation

The process of breaking down fatty acids into acetyl-CoA, which can then be used to produce energy.

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How do free fatty acids affect beta-oxidation?

Increase in free fatty acid levels lead to increased beta-oxidation.

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How does insulin affect beta-oxidation?

Insulin, primarily released after a meal, inhibits beta-oxidation and promotes fatty acid storage.

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How does glucagon affect beta-oxidation?

Glucagon, released during fasting, stimulates beta-oxidation and lipolysis to provide energy.

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What is the role of CPT I in beta-oxidation?

CPT I, an enzyme involved in fatty acid transport, is inhibited by malonyl-CoA, preventing fatty acid entry into mitochondria where they are broken down.

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What are ketone bodies?

Water-soluble molecules produced by the liver from fatty acids during low carbohydrate availability.

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What is ketogenesis?

Ketogenesis is the process of creating ketone bodies from fatty acids.

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What is the function of ketone bodies?

Ketone bodies are used as energy sources by tissues, especially the brain, during times of glucose scarcity.

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What is heme degradation?

The process of breaking down heme into bilirubin, a yellow pigment, for excretion.

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Where does heme degradation begin?

Heme degradation starts in macrophages, where heme is released from hemoglobin.

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What is the first step in heme degradation?

Heme is converted to biliverdin, a green pigment, by the enzyme heme oxygenase.

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How is biliverdin converted to bilirubin?

Biliverdin is then reduced to bilirubin, a yellow pigment, by the enzyme biliverdin reductase.

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What happens to bilirubin after its formation?

Bilirubin is transported to the liver, conjugated with glucuronic acid, and excreted in bile.

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What is Hemoglobin?

Hemoglobin is a protein found in red blood cells that plays a crucial role in oxygen transport throughout the body.

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Globin Proteins

Globin proteins are globular proteins found in hemoglobin, forming the structure of the molecule. They are responsible for the shape and stability of hemoglobin.

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Heme Group

A heme group is a molecule that contains a ring-like structure (porphyrin) and an iron atom at its center, found within each globin chain of hemoglobin.

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Iron Atom in Heme

The iron atom in the heme group is crucial for oxygen binding. It can bind one oxygen molecule. One hemoglobin molecule can bind up to four oxygen molecules because it has four heme groups.

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How does Hemoglobin Transport Oxygen?

Hemoglobin binds to oxygen in the lungs, where oxygen levels are high, and releases it in the tissues, where oxygen levels are low. This is crucial for providing cells with the oxygen they need to function.

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What else does Hemoglobin do besides oxygen?

Hemoglobin also transports carbon dioxide from tissues back to the lungs for exhalation. This is a crucial part of removing waste products from the body.

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Oxygen-Binding Sites in Hemoglobin

The binding of oxygen molecules to hemoglobin occurs at the iron atom within the heme groups. This binding is reversible, meaning oxygen can attach and detach when needed.

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Cooperative Binding in Hemoglobin

When one oxygen molecule binds to hemoglobin, it increases the affinity of the remaining binding sites for oxygen. This cooperative binding allows hemoglobin to efficiently load up with oxygen in the lungs.

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Study Notes

Final Exam Information

  • Duration: 2 hours
  • Exam type: Closed-book
  • Calculators: Bring non-programmable calculators according to HKMU approved list
  • Topics covered: Lectures 1-11 (mainly focus on lectures 6-11)
  • Weight: 50% of overall grade

Final Exam Structure

  • Multiple Choice Questions (20%): 20 questions, each worth 1 mark
  • Short Questions (40%): 7 questions, marks vary by question
  • Long Questions (40%): 5 questions, each worth 10 marks, select 4 to answer

Example of Short Questions

  • Name the metabolite or enzyme from 1 to 6 in the provided diagram of the TCA cycle (diagram on page 4)
  • Name five important enzymes in oxidative phosphorylation. Give one disorder related to dysfunction of oxidative phosphorylation. (page 5)
  • What are the overall products of the TCA cycle? How do these products contribute to energy production? (page 5)
  • Describe the four levels of protein structure. (page 5)

Example of Long Questions

  • A 45-year-old male presents to the emergency department after several days of severe fasting and significant weight loss. He has a type 2 diabetes history and reports fatigue, weakness, and confusion. Blood tests reveal elevated ketone levels and high blood urea nitrogen. Identify two metabolic processes regarding the elevated ketone levels and high blood urea nitrogen in this patient. (page 6)
  • How will the activity of acyl-CoA dehydrogenase change in this patient? Why? (page 6)
  • For patients with type 2 diabetes, insulin levels often become insufficient to effectively manage blood glucose utilization. What is the most likely disorder this patient will develop if his diabetic condition is not well-controlled? Why? (page 6)

Lecture 1: Water and Aqueous System

  • Chemical formula: H2O
  • Water is a polar molecule
  • Polarity allows hydrogen bonding between water molecules.
  • Important properties: Cohesion, adhesion, high boiling point, high specific heat, and excellent solvent for polar molecules
  • Water can act as an acid or a base due to its polar structure.
  • Autoionization of water: H2O + H2O ↔ H3O+ + OH
  • Equilibrium constant (Kw) at 25°C: 1.0 x 10-14
  • In pure water: [H+] = [OH] = 1.0 x 10-7 M
  • Buffers resist changes in pH.
  • A buffer is a weak acid and its conjugate base, or a pair of a weak base and its conjugate acid.
  • Examples of buffers: phosphate buffers

Lecture 2: Carbohydrates, Proteins, and Lipids

  • Carbohydrates: glucose, galactose, mannose, fructose, ribose, deoxyribose
  • Monosaccharides: single sugar units
  • Disaccharides: two sugar units linked together
  • Oligosaccharides: 3-10 sugar units
  • Polysaccharides: many sugar units
  • Proteins: composed of amino acids, 9 non-polar and 6 polar amino acids also includes positively and negatively charged amino acids; Primary, Secondary, Tertiary, Quaternary structure
  • Lipids: Glycerophospholipids, Sphingolipids, Glycolipids, Fatty Acids (saturated and unsaturated (monounsaturated, polyunsaturated));
  • Polyunsaturated fatty acids (PUFAs), including omega-3 and omega-6 fatty acids

Lecture 3: Nucleic Acids

  • DNA: double helix structure, made of deoxyribose sugar and phosphate groups, with bases (A, T, C, G). Adenine pairs with thymine, guanine pairs with cytosine
  • RNA: Single stranded structure, made of ribose sugars and phosphate groups, with bases (A, U, C, G). Adenine pairs with uracil, and guanine pairs with cytosine
  • Functions of DNA: store genetic information, transmit genetic material
  • Functions RNA: instruction of protein synthesis, various roles in protein synthesis

Lecture 4: Metabolism and Energy I: TCA Cycle

  • The TCA cycle is a series of chemical reactions in the mitochondrial matrix that oxidizes acetyl-CoA, producing energy (ATP)
  • Acetyl-CoA is a key intermediate in linking glycolysis and the TCA cycle.
  • Products of each acetyl-CoA molecule in the TCA cycle are 2 CO2, 3 NADH, 1 FADH2, 1 GTP/ATP.
  • TCA cycle roles: energy production, formation of metabolic intermediates, linking metabolic pathways

Lecture 5: Metabolism and Energy II: Oxidative Phosphorylation

  • ATP production process via electron transport chain
  • Electron transport chain (ETC) uses energy from electrons to create a proton gradient
  • Chemiosmosis: protons move back across the inner mitochondrial membrane, driving ATP synthesis
  • Function of oxidative phosphorylation: ATP production, cellular respiration integration, metabolic regulation, heat generation

Lecture 6: Carbohydrate Metabolism: Part I - Glycolysis

  • Glycolysis: breakdown of glucose to pyruvate in the cytoplasm
  • Two phases of glycolysis: preparatory phase (steps 1-5), payoff phase (steps 6-10)
  • Key steps: glucose phosphorylation, isomerization, phosphorylation, cleavage, isomerization, oxidation, transfer of phosphate, isomerization, dehydration, transfer of phosphate
  • Glycolysis products: 2 pyruvate, 2 NADH, and 2 ATP
  • Glycolysis regulation: influenced by substrate availability, feedback inhibition

Lecture 7: Protein and Lipid Metabolism

  • Protein and lipid metabolism are critical parts of overall metabolism.
  • The catabolism of various biomolecules converts them into usable energy intermediates.

Lecture 8: Hemoglobin

  • Hemoglobin: a globular protein in red blood cells that transports oxygen through blood
  • Basic components: globin chains (alpha and beta), heme group, iron atom
  • Function: oxygen transport, carbon dioxide transport, pH regulation

Lecture 9: Enzyme I: Introduction to Enzymes

  • Enzymes are biological catalysts that speed up biochemical reactions
  • They act by lowering activation energy
  • Enzymes have specific active sites for substrate binding.

Lecture 10: Enzyme II: Enzyme Kinetics and Inhibitors

  • Enzyme kinetics: study of enzyme reaction rates and their dependence on substrate concentration
  • Michaelis-Menten equation: describes the relationship between reaction velocity, substrate concentration, and enzyme properties
  • Enzyme inhibitors: molecules that can bind to the enzyme and reduce its activity

Lecture 11: Enzyme III: Enzyme Diagnostics and Assay

  • Liver enzymes, cardiac enzymes, and pancreatic enzymes in diagnostics

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