Enzymes: Biochemistry

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Questions and Answers

How do enzymes catalyze reactions?

  • By increasing the overall energy change (\$\Delta G\$) of the reaction.
  • By providing energy to the reactants.
  • By lowering the activation energy required for the reaction. (correct)
  • By increasing the activation energy required for the reaction.

An enzyme's active site and allosteric site differ in that the active site is where the:

  • noncompetitive inhibitor binds.
  • substrate binds and reaction occurs. (correct)
  • enzyme undergoes irreversible conformational change.
  • enzyme is synthesized.

Which factor does NOT directly influence enzyme function?

  • Substrate concentration
  • Temperature
  • Atmospheric pressure (correct)
  • pH

What is 'induced fit' in enzyme catalysis?

<p>The change in enzyme shape upon substrate binding, which optimizes the fit between the enzyme and substrate. (B)</p> Signup and view all the answers

How does a competitive inhibitor decrease the rate of an enzyme reaction?

<p>By binding to the active site, preventing the substrate from binding. (A)</p> Signup and view all the answers

Activators increase enzyme activity by:

<p>Binding to an allosteric site and stabilizing the active form of the enzyme. (D)</p> Signup and view all the answers

What is allosteric regulation of enzymes?

<p>Regulation by a molecule binding at a site other than the active site, affecting enzyme activity. (D)</p> Signup and view all the answers

Which of the following catabolic pathways yields the most ATP per glucose molecule?

<p>Aerobic cellular respiration (A)</p> Signup and view all the answers

In cellular respiration, what molecule is reduced and what molecule is oxidized?

<p>Oxygen is reduced and glucose is oxidized. (B)</p> Signup and view all the answers

What is the primary role of oxygen in cellular respiration?

<p>To act as the final electron acceptor in the electron transport chain. (D)</p> Signup and view all the answers

Which of the following correctly describes a redox reaction?

<p>The pairing of an oxidation reaction with a reduction reaction. (D)</p> Signup and view all the answers

What is the oxidizing agent in the following reaction: $NAD^+ + 2e^- + 2H^+ \rightarrow NADH + H^+$?

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

In which stage of aerobic respiration is ATP produced by substrate-level phosphorylation only?

<p>Citric acid cycle and glycolysis (D)</p> Signup and view all the answers

What is the net gain of ATP from glycolysis per glucose molecule?

<p>2 ATP (B)</p> Signup and view all the answers

What is produced during pyruvate oxidation?

<p>Acetyl CoA and $CO_2$ (A)</p> Signup and view all the answers

What is produced from one turn of the citric acid cycle?

<p>1 ATP, 3 NADH, and 1 FADH2 (A)</p> Signup and view all the answers

Chemiosmosis is best defined as:

<p>The movement of ions down their electrochemical gradient to synthesize ATP. (B)</p> Signup and view all the answers

During cellular respiration, energy flows from:

<p>Glucose -&gt; NADH/FADH2 -&gt; Electron Transport Chain -&gt; ATP (B)</p> Signup and view all the answers

How is fermentation different from cellular respiration?

<p>Fermentation does not use oxygen, while cellular respiration usually does. (B)</p> Signup and view all the answers

In alcohol fermentation, what is the final electron acceptor?

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

Flashcards

What are enzymes?

Biological molecules (usually proteins) that significantly speed up the rate of virtually all of the chemical reactions that take place within cells. They lower the activation energy required for a reaction to occur.

Enzyme Sites

The active site is where the substrate binds and the catalytic action occurs. The allosteric site is a different location on the enzyme where a molecule can bind and influence the enzyme's activity.

Factors affecting Enzyme Function

Enzyme activity is affected by temperature, pH, enzyme concentration, substrate concentration, and the presence of any inhibitors or activators.

What is 'induced fit'?

The change in shape of the active site of an enzyme so that it binds more snugly to the substrate, induced by entry of the substrate.

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Competitive vs. Noncompetitive Inhibition

Competitive inhibition involves a molecule similar to the substrate binding to the active site, blocking the substrate. Noncompetitive (allosteric) inhibition involves a molecule binding to a different site, changing the enzyme's shape and reducing its activity.

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Activators and Inhibitors

Activators bind to the enzyme and stabilize the active form, increasing activity. Inhibitors bind and stabilize the inactive form, decreasing activity.

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Allosteric Regulation

The regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site.

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Catabolic Pathways

Glycolysis, fermentation, and cellular respiration.

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Cellular Respiration: Reactants & Products

Cellular respiration uses glucose and oxygen to produce carbon dioxide, water, and ATP. Oxygen is reduced, and glucose is oxidized.

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Fuel for Cellular Respiration

Carbohydrates, fats, and proteins can all be used as fuel.

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What is Redox Reaction?

A chemical reaction involving the transfer of one or more electrons from one reactant to another; also called oxidation-reduction reaction.

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Oxidizing vs. Reducing Agent

An oxidizing agent accepts electrons and is reduced. A reducing agent donates electrons and is oxidized.

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Electron Acceptors

NAD+ and FAD are the two main electron acceptors.

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Stages of Aerobic Respiration

Glycolysis, Pyruvate Oxidation and the Citric Acid Cycle, and Oxidative Phosphorylation.

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Glycolysis Summary

Glycolysis: glucose is split into two pyruvate molecules, producing 2 ATP (net) and 2 NADH.

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Pyruvate Oxidation

Pyruvate is oxidized to Acetyl CoA, producing NADH and releasing CO2.

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Citric Acid Cycle (Krebs Cycle)

Citric acid cycle: Acetyl CoA is further oxidized, producing ATP, NADH, FADH2, and releasing CO2.

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Substrate-Level Phosphorylation

Substrate-level phosphorylation is the direct transfer of a phosphate group from an organic substrate to ADP by an enzyme.

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The Electron Transport Chain

The electron transport chain (ETC) transfers electrons from NADH and FADH2 to oxygen, releasing energy to pump protons and create a gradient.

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Chemiosmosis

Chemiosmosis uses the proton gradient created by the ETC to drive ATP synthase, phosphorylating ADP to ATP.

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Study Notes

Enzymes

  • Enzymes are proteins that act as catalysts to speed up biochemical reactions.
  • Enzymes lower the activation energy of a reaction, making it easier to occur.

Enzyme-Catalyzed Reaction Diagram

  • With an enzyme, the free energy diagram would show a lower activation energy peak compared to the uncatalyzed reaction.

Enzyme Active Sites

  • Active site: Where the substrate binds and the reaction occurs.
  • Allosteric site: Where molecules can bind to regulate enzyme activity (noncompetitive inhibitors or activators).

Factors Affecting Enzyme Function

  • Temperature: Enzymes have an optimal temperature range; high temperatures can denature the enzyme
  • pH: Enzymes have an optimal pH range; deviations can disrupt enzyme structure and function.
  • Substrate Concentration: Increasing substrate concentration increases reaction rate until saturation.
  • Inhibitors and Activators: These molecules can decrease or increase enzyme activity, respectively.

Induced Fit

  • "Induced fit" refers to the conformational change an enzyme undergoes upon substrate binding, which results in tighter binding of the substrate to the active site and enhances the reaction.

Enzyme Inhibition

  • Competitive inhibition: An inhibitor binds to the active site, blocking substrate binding.
  • Noncompetitive/Allosteric inhibition: An inhibitor binds to an allosteric site, changing the enzyme's shape and reducing its activity.

Enzyme Regulation

  • Activators bind to an enzyme and stabilize the active form, increasing its activity.
  • Inhibitors bind to an enzyme and stabilize the inactive form, decreasing its activity.

Allosteric Regulation

  • Allosteric regulation is when a regulatory molecule binds to an enzyme at one site (allosteric site) and affects the function of the enzyme at a different site (active site).

Catabolic Pathways

  • Three pathways: Fermentation, Anaerobic respiration, and Aerobic/Cellular respiration.
  • Fermentation: Partial degradation of sugars that occurs without oxygen.
  • Anaerobic respiration: Similar to aerobic respiration but uses other substances than oxygen to accept electrons.
  • Aerobic/Cellular respiration: Complete breakdown of organic molecules with oxygen, yielding more ATP.

Cellular Respiration

  • Reactants: Glucose (C6H12O6) and Oxygen (O2).
  • Products: Carbon Dioxide (CO2), Water (H2O), and ATP.
  • Glucose is oxidized to CO2.
  • Oxygen is reduced to Water.

Cellular Respiration Fuel

  • Can be fueled by carbohydrates, fats, and proteins.

Redox Reactions

  • Redox reaction: A chemical reaction involving the transfer of electrons between two species.
  • Oxidation: The loss of electrons from a substance.
  • Reduction: The gain of electrons to a substance.

Oxidizing and Reducing Agents

  • Oxidizing agent: The substance that accepts electrons (is reduced).
  • Reducing agent: The substance that donates electrons (is oxidized).

Electron Acceptors

  • Aerobic/Cellular respiration: Oxygen (O2)
  • Anaerobic respiration: Sulfate, nitrate and sulfur

Stages of Aerobic/Cellular Respiration

  • Glycolysis
  • Pyruvate Oxidation and Citric Acid Cycle (Krebs Cycle)
  • Oxidative Phosphorylation (Electron Transport Chain and Chemiosmosis)

Glycolysis

  • Input: Glucose, 2 ATP
  • Output: 2 Pyruvate, 2 NADH, 4 ATP (net gain of 2 ATP)
  • Products/Net Yield: 2 ATP (net), 2 NADH, 2 Pyruvate
  • Location: Cytosol.
  • ATP Production: Substrate-level phosphorylation.

Pyruvate Oxidation

  • Input: 2 Pyruvate
  • Output: 2 Acetyl CoA, 2 CO2, 2 NADH
  • Products/Net Yield: 2 Acetyl CoA, 2 NADH, 2 CO2
  • Location: Mitochondrial matrix.
  • ATP Production: None directly.

Citric Acid Cycle (Krebs Cycle)

  • Input: 2 Acetyl CoA
  • Output: 4 CO2, 6 NADH, 2 FADH2, 2 ATP
  • Products/Net Yield (per 1 Acetyl CoA): 1 ATP, 3 NADH, 1 FADH2, 2 CO2
  • Products/Net Yield (per 2 Acetyl CoA): 2 ATP, 6 NADH, 2 FADH2, 4 CO2
  • Location: Mitochondrial matrix.
  • ATP Production: Substrate-level phosphorylation.

Oxidative Phosphorylation

  • Consists of the Electron Transport Chain and Chemiosmosis.

Electron Transport Chain (ETC)

  • Structure: A series of protein complexes embedded in the inner mitochondrial membrane.
  • Function: Accepts electrons from NADH and FADH2, passes them down the chain, and uses the energy to pump protons (H+) across the inner mitochondrial membrane.
  • Purpose: Creates a proton gradient that drives ATP synthesis via chemiosmosis.

Chemiosmosis

  • Mechanism: H+ ions flow down their concentration gradient through ATP synthase, a protein complex in the inner mitochondrial membrane.
  • Enzyme Involved: ATP synthase.
  • End Result: The energy from the H+ gradient is used to phosphorylate ADP, producing ATP.

Energy Flow in Cellular Respiration

  • Glucose → NADH/FADH2 → Electron Transport Chain → Proton-Motive Force → ATP

Anaerobic Respiration

  • Differs from aerobic respiration by using a final electron acceptor other than oxygen (e.g., sulfate, nitrate).

Fermentation

  • Similar to anaerobic respiration in that it doesn't use oxygen.
  • Different from anaerobic respiration because it does not involve an electron transport chain.

Fermentation

  • Consists of glycolysis plus reactions that regenerate NAD+, which can then be reused by glycolysis.

Types of Fermentation

  • Alcohol Fermentation:
    • Final electron acceptor: Acetaldehyde.
    • Product: Ethanol and CO2.
  • Lactic Acid Fermentation:
    • Final electron acceptor: Pyruvate.
    • Product: Lactate.

Regulation of Catabolism

  • Cells regulate catabolism through feedback inhibition, where the end product of a metabolic pathway inhibits an enzyme early in the pathway.

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