Respiration

Page 1: Overview of Aerobic Respiration and Metabolic Pathways

Key Components in Energy Production

  • Citrate: Important in the citric acid cycle; it transfers energy through intermediates (e.g., via Acetyl CoA).

  • Acetyl CoA: A central molecule in metabolism that transitions pyruvate into the citric acid cycle.

  • NADH & FADH: Electron carriers that transport electrons to the electron transport chain.

Inhibition and Stimulation Factors

  • Inhibited by ATP and high energy molecules (e.g., succinyl CoA).

  • Stimulated by ADP and CO2, indicating energy needs.

Page 2: Learning Goals

  • Regions of Mitochondria: Identify and describe functions.

  • Conversion of Pyruvate to Acetyl CoA: Understand location and components of pyruvate dehydrogenase complex.

  • Aerobic Respiration Summary: Summarize key reactions.

  • Control of the Citric Acid Cycle: Mechanisms of regulation.

  • Oxidative Phosphorylation: Explain importance and mechanism.

  • Amino Acids in Citric Acid Cycle: Conversion processes.

  • Urea Cycle: Importance and steps.

  • Hyperammonemia: Causes, effects, and significance.

  • Role of the Citric Acid Cycle: Overview in catabolism and anabolism.

Page 3: Overview of Catabolic Processes

  • Nutrients (carbohydrates, fats, proteins) release energy through catabolism.

  • Carbohydrates are a primary energy source.

Page 4: Structure of Mitochondria

  • Mitochondria: Dual membrane, highly folded structure (cristae).

  • Membrane Parts:

    • Outer membrane: More permeable.

    • Inner membrane: Houses ATP synthase and electron transport system.

    • Matrix: Site for citric acid cycle, beta-oxidation, and amino acid degradation.

Page 5: Pyruvate to Acetyl CoA Conversion

  • Under aerobic conditions, pyruvate is converted to acetyl CoA in mitochondria.

  • Conversion activates acetyl for the citric acid cycle (Krebs cycle).

Page 6: Acetyl CoA Formation

  • Pyruvate enters the mitochondria; undergoes conversion to a 2-carbon acetyl group.

  • Activation through bonding with coenzyme A via high-energy thioester bond.

Page 7: Decarboxylation and Oxidation of Pyruvate

  • Steps:

    1. Decarboxylation (loss of CO2).

    2. Oxidation using NAD, producing NADH.

    3. Acetyl group linked to coenzyme A.

  • Involves 3 enzymes and 5 coenzymes bundled in the pyruvate dehydrogenase complex.

Page 8: Detailed Decarboxylation & Oxidation

  • Same steps as Page 7 emphasized: loss of carboxyl group, oxidation, and thioester bond formation.

Page 9: Pyruvate Dehydrogenase Complex

  • Comprising 5 coenzymes (4 vitamin-derived) and 3 enzymes:

    • Thiamine pyrophosphate (from thiamine).

    • FAD (from riboflavin).

    • NAD (from niacin).

    • Coenzyme A (from pantothenic acid).

    • Lipoamide.

Page 10: Role of Acetyl CoA in Metabolism

  • Central in metabolism, transporting acetyl group to the citric acid cycle.

  • Also functions in biosynthetic reactions for cholesterol and fatty acid production.

  • Interconversion of energy from fats, proteins, and carbohydrates.

Page 11: Overview of Aerobic Respiration

  • Breakdown of food with oxygen, producing ATP, via oxidative phosphorylation.

  • Performed in the mitochondrial matrix.

  • Involves oxidations transferring hydride to NAD or FAD, with electron transport to O2.

Page 12: The Citric Acid Cycle

  • Final stage of nutrient breakdown.

  • Acetyl CoA and oxaloacetate initiate the cycle.

  • Acetyl oxidized to CO2 and electrons transferred to NAD and FAD.

  • Involves 8 enzymatic steps with allosteric control.

Page 13: Details of the Citric Acid Cycle

  • Emphasizes dietary nutrient breakdown and energy production: Acetyl CoA + oxaloacetate generating NADH and FADH2.

Page 14: Control of the Citric Acid Cycle

  • Responds to energy needs; accelerates when ATP demand increases.

  • Four key enzymes regulated allosterically.

Page 15: Allosterically Regulated Reactions

  • Key steps:

    • Pyruvate to Acetyl CoA influenced by ATP/NADH levels.

    • Synthesis of citrate is negatively affected by ATP.

    • Isocitrate to α-ketoglutarate regulated by ADP and inhibited by NADH/ATP levels.

    • α-Ketoglutarate to succinyl CoA influenced by ATP/Succinyl CoA/NADH.

Page 16: Oxidative Phosphorylation

  • Respiratory electron transport system consists of electron carriers in the inner mitochondrial membrane.

  • NADH yields 3 ATP; FADH2 yields 2 ATP.

  • ATP synthesis via ATP synthase (F0F1 complex).

Page 17: Energy Yield from Glucose

  • Summary of ATP yield from glycolysis, pyruvate conversion, and citric acid cycle.

  • Total net ATP: 36.

Page 18: Electron Transport Systems

  • Carbohydrates, fats, proteins release energy, primarily using carbohydrates.

Page 19: Electron Transport Systems Overview

  • Components include coenzymes and cytochromes in the mitochondrial membrane, organized for electron transfers.

Page 20: The Hydrogen Ion Gradient

  • Protons pumped from matrix to intermembrane space contribute to a high-energy H+ reservoir, facilitating ATP production.

  • NADH dehydrogenase transfers electrons across all 3 sites; FADH2 oxidation across 2 sites.

Page 21: Electron Flow Through Electron Carriers

  • Flow of electrons in the electron transport system, leading to ATP synthesis.

Page 22: NADH and ATP Production

  • NADH transports electrons into the electron transport system, generating ATP through proton pumps.

Page 23: ATP Synthase Function

  • Protons flow through ATP synthase's F0 channel to catalyze ATP phosphorylation from ADP.

Page 24: Amino Acid Catabolism

  • Catabolism of proteins for energy, with carbohydrates as primary fuels.

Page 25: Degradation of Amino Acids

  • In starvation, amino acids are degraded for energy in the liver through transamination and carbon skeleton degradation.

Page 26: Transamination Process

  • Transfer of α-amino group by transaminase, often involving α-ketoglutarate.

Page 27: Pyridoxal Phosphate

  • Coenzyme for transamination, derived from vitamin B6 (pyridoxine).

Page 28: Aspartate Transaminase

  • Catalyzes aspartate's α-amino group transfer to produce oxaloacetate and glutamate.

Page 29: Alanine Transaminase

  • Transfers alanine's α-amino group to α-ketoglutarate, producing pyruvate and glutamate.

Page 30: Oxidative Deamination

  • Breakdown of glutamate through glutamate dehydrogenase, liberating ammonium ion.

Page 31: Deamination of an α-Amino Acid

  • Conversion process involving ammonium ions and Urea Cycle participation.

Page 32: Amino Acid Metabolism Diagram

  • Various amino acids degrade into key metabolic intermediates like Acetyl CoA and others.

Page 33: The Urea Cycle

  • Critical for removing toxic ammonium ions produced during amino acid breakdown.

  • Urea is formed and excreted; enzyme deficiencies can lead to hyperammonemia.

Page 34: Urea Cycle Pathway

  • Diagram illustrating key components and steps in urea cycle mechanics.

Page 35: Ammonia Toxicity

  • High ammonia levels are toxic; converted to urea for safe excretion through kidneys.

Page 36: Dual Function of the Citric Acid Cycle

  • Functions in both catabolism and anabolism; intermediates can be transformed into amino acids.

Page 37: Pathways for Biosynthetic Precursors

  • Citric acid cycle provides intermediates for synthesizing various molecules like glucose, nucleotides, and lipids.

Page 38: Overview of Amino Acid and Fatty Acid Metabolism

  • Integration of metabolic pathways for amino acids, fatty acids, and carbohydrates, showing interconnected biosynthetic pathways.