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Questions and Answers
Which of the following statements about peroxidases is true?
Which of the following statements about peroxidases is true?
What role does superoxide dismutase serve in aerobic organisms?
What role does superoxide dismutase serve in aerobic organisms?
Where are the components of the electron transport chain located?
Where are the components of the electron transport chain located?
Which complex in the electron transport chain is not a proton pump?
Which complex in the electron transport chain is not a proton pump?
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What is the final electron acceptor in the electron transport chain?
What is the final electron acceptor in the electron transport chain?
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Which component of peroxidases uses hydrogen peroxide as both an electron donor and acceptor?
Which component of peroxidases uses hydrogen peroxide as both an electron donor and acceptor?
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Glutathione peroxidase primarily protects what part of the cell?
Glutathione peroxidase primarily protects what part of the cell?
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What is the primary function of the electron transport chain?
What is the primary function of the electron transport chain?
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What is the primary function of oxygenases in biochemical reactions?
What is the primary function of oxygenases in biochemical reactions?
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Which type of oxygenase incorporates both atoms of molecular oxygen into the substrate?
Which type of oxygenase incorporates both atoms of molecular oxygen into the substrate?
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What does a more negative Eo value indicate about a substance's ability to participate in redox reactions?
What does a more negative Eo value indicate about a substance's ability to participate in redox reactions?
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Which of the following statements accurately describes dehydrogenases?
Which of the following statements accurately describes dehydrogenases?
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What type of oxygenase is also known as a mixed-function oxidase?
What type of oxygenase is also known as a mixed-function oxidase?
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In terms of redox potential, which of the following statements is true?
In terms of redox potential, which of the following statements is true?
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What are the products formed by the action of monooxygenases?
What are the products formed by the action of monooxygenases?
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Which of the following examples is a dioxygenase?
Which of the following examples is a dioxygenase?
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What type of coenzymes do pyridine-linked dehydrogenases utilize?
What type of coenzymes do pyridine-linked dehydrogenases utilize?
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What is the primary function of dehydrogenases in cell metabolism?
What is the primary function of dehydrogenases in cell metabolism?
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Which of the following molecules is not considered an electron carrier in the inner mitochondrial membrane?
Which of the following molecules is not considered an electron carrier in the inner mitochondrial membrane?
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What distinguishes dioxygenases from monooxygenases?
What distinguishes dioxygenases from monooxygenases?
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Which characteristic of a reductant is indicated by a more negative Eo?
Which characteristic of a reductant is indicated by a more negative Eo?
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What advantage do reducing equivalents provide in oxidative processes?
What advantage do reducing equivalents provide in oxidative processes?
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Which of these is not one of the electron carriers found in the electron transport assembly?
Which of these is not one of the electron carriers found in the electron transport assembly?
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What role do components of the electron transport chain (ETC) play concerning dehydrogenases?
What role do components of the electron transport chain (ETC) play concerning dehydrogenases?
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Which complex in the electron transport chain is NOT considered a proton pump?
Which complex in the electron transport chain is NOT considered a proton pump?
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What is the role of CoQ in the electron transport chain?
What is the role of CoQ in the electron transport chain?
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Which of the following components serves as the prosthetic group in complex I?
Which of the following components serves as the prosthetic group in complex I?
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What type of proteins are found in complexes I, II, and III that are involved in electron transfer?
What type of proteins are found in complexes I, II, and III that are involved in electron transfer?
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During oxidative phosphorylation, which molecule is phosphorylated to form ATP?
During oxidative phosphorylation, which molecule is phosphorylated to form ATP?
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Which iron state is reduced to donate electrons to cytochrome c?
Which iron state is reduced to donate electrons to cytochrome c?
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What is cytochrome b's role in complex III?
What is cytochrome b's role in complex III?
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Which vitamin is a precursor for the flavoprotein FAD?
Which vitamin is a precursor for the flavoprotein FAD?
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What is the role of cytochrome c in the electron transport chain?
What is the role of cytochrome c in the electron transport chain?
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Which type of iron is cytochrome b converted back to after being oxidized?
Which type of iron is cytochrome b converted back to after being oxidized?
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Which enzyme is NOT an example of a NAD-linked dehydrogenase?
Which enzyme is NOT an example of a NAD-linked dehydrogenase?
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What does FADH2 carry compared to NADH?
What does FADH2 carry compared to NADH?
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Which of the following correctly characterizes Fe2+ in cytochrome c?
Which of the following correctly characterizes Fe2+ in cytochrome c?
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What is a characteristic of complex III in the context of the electron transport chain?
What is a characteristic of complex III in the context of the electron transport chain?
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What products does reduced NADH generate during metabolic pathways?
What products does reduced NADH generate during metabolic pathways?
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Which enzyme is associated with the beta oxidation pathway?
Which enzyme is associated with the beta oxidation pathway?
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Study Notes
Dehydrogenase
- Measures a biological system's tendency to release or accept electrons
- Transfers hydrogen from one substrate to another, but not to oxygen
- Expressed in volts (Eo)
- More negative Eo: better reductant (electron donor)
- More positive Eo: better oxidant (electron acceptor)
Redox Potential in Mammalian Oxidation Systems
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Types of Dehydrogenases:
-
Pyridine-linked dehydrogenases: use niacin derivatives as coenzymes
- Nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenases: involved in oxidative metabolic pathways generating ATP (e.g., peroxidases)
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Flavoprotein dehydrogenases: use flavins (FMN & FAD) as coenzymes
- FAD-linked dehydrogenases: involved in the citric acid cycle and fatty acid metabolism.
- FMN-linked dehydrogenases: involved in the electron transport chain.
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Pyridine-linked dehydrogenases: use niacin derivatives as coenzymes
Catalase
- Uses hydrogen peroxide as both electron donor and acceptor to form water
- Found in blood, bone marrow, mucous membranes, kidney, and liver
- Destroys H2O2 formed by oxidases
Oxygenases
- Catalyze the direct transfer and incorporation of oxygen into a substrate molecule
-
Two Kinds of Oxygenases:
- Dioxygenases: incorporate both atoms of molecular oxygen into the substrate (e.g. homogentisate, L-tryptophan, and hydroxyanthranilate dioxygenases)
- Monooxygenases (Mixed-function oxidases/Hydroxylases): incorporate only one atom of molecular oxygen into the substrate.
Superoxide Dismutase
- Protects aerobic organisms against oxygen toxicity
- Catalyzes the removal of superoxide by the following reaction: O2.- + O2.- + 2H+ → H2O2 + O2
Electron Transport Chain (Respiratory Chain)
- Found in the inner mitochondrial membrane
- Collects and transports reducing equivalents (electrons) and directs them to their final reaction with oxygen to form water
- Final acceptor of electrons is oxygen
- Components:
- Four large protein complexes (I, II, III, IV)
- Three complexes serve as proton pumps (I, III, IV)
- Complex II is not a proton pump
- Coupled with oxidative phosphorylation
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Components of ETC
-
Flavoproteins:
- Components of complexes I & II
- FMN: Prosthetic group of NADH dehydrogenase in complex I
- FAD: Prosthetic group of succinate dehydrogenase in complex II
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Iron-sulfur proteins (non-heme, Fe-S):
- Found in complexes I, II, and III
- Participate in single electron transfer reaction
-
Flavoproteins:
-
Electron Carriers:
-
NAD: Derived from niacin (vitamin B3), active portion: nicotinamide ring, carries 2 electrons but only one H+, carrier of reduced NADH
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Reduced NADH derived from NAD-linked dehydrogenases:
- Isocitrate, α-ketoglutarate, & malate dehydrogenases of the Krebs cycle
- Pyruvate dehydrogenase (linking glycolysis to the TCA cycle)
- Hydroxyacyl CoA dehydrogenase of the fatty acid beta-oxidation pathway.
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Reduced NADH derived from NAD-linked dehydrogenases:
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FAD: Derived from riboflavin (vitamin B2), active portion: isoalloxazine ring, carries 2 electrons and 2 H+, carrier of reduced FADH2
-
Reduced FADH2 derived from FAD-linked dehydrogenases:
- Succinate dehydrogenase of the TCA cycle
- Alpha-glycerophosphate shuttle dehydrogenase
- Fatty acyl CoA dehydrogenase of beta oxidation
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Reduced FADH2 derived from FAD-linked dehydrogenases:
-
NAD: Derived from niacin (vitamin B3), active portion: nicotinamide ring, carries 2 electrons but only one H+, carrier of reduced NADH
Complex III
- Cytochrome b: Representative cytochrome in complex III. Other cytochromes can be used as carriers
- CoQH2 (reduced substrate): Transfers its electron to the ferric iron (Fe3+) of cytochrome b. CoQH2 is oxidized to CoQ upon transferring electrons
- Fe3+ is reduced to ferrous iron (Fe2+) which serves as the electron donor and transfers the electron to ferric iron (Fe3+) of cytochrome c.
- Fe2+ of cytochrome b converts back to Fe3+ while Fe3+ of cytochrome c is reduced to Fe2+
- Cytochrome c links complex III to complex IV
- Complex III is a proton pump.
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Description
Explore the roles of dehydrogenases in biological systems, including their function in transferring hydrogen and their significance in oxidation-reduction processes. Learn about different types of dehydrogenases, such as pyridine-linked and flavoprotein dehydrogenases, and their involvement in metabolic pathways. Dive into the intricacies of redox potential measurements expressed in volts.