Nitrogen Metabolism
NIOS · Class 12 · Biology
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During biological nitrogen fixation, the enzyme nitrogenase requires 16 ATP molecules to reduce one molecule of N₂. Which of the following correctly describes the stepwise reduction pathway of nitrogen to ammonia?
Leghemoglobin is a unique protein found in root nodules of legumes. Which of the following statements BEST explains why leghemoglobin is described as a product of symbiosis?
Nitrate reductase enzyme is described as 'inducible'. What happens to the synthesis of nitrate reductase when excess NH₄⁺ accumulates in plant cells?
In which cellular organelle does the reduction of nitrite to ammonia take place in plant cells?
Sample Questions
Which of the following organisms demonstrates a non-leguminous symbiotic nitrogen fixation system involving an actinomycete?
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Alnus and actinomycete
Step 1: Symbiotic nitrogen fixation occurs in various plant-microbe associations. Step 2: The most well-known is legumes (angiosperms) with Rhizobium. Step 3: However, some non-leguminous angiosperms like Alnus, Myrica, and Purshia also fix nitrogen symbiotically — but their symbiont is an actinomycete, not Rhizobium. Step 4: Azolla-Anabaena is a pteridophyte-cyanobacteria association. Cycas-Cyanobacteria is a gymnosperm association. Digitaria-Azospirillum is another angiosperm-bacteria association. Step 5: Therefore, Alnus with actinomycete is the correct non-leguminous symbiotic system with
The overall equation for biological nitrogen fixation is: N₂ + 16ATP + 8H⁺ + 8e⁻ → 2NH₃ + 16ADP + 16Pi + H₂. What does the presence of H₂ as a product indicate?
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One pair of electrons is used to reduce 2H⁺ to H₂ instead of reducing N₂, indicating some energy loss.
Step 1: In the nitrogen fixation equation, 8 electrons (8e⁻) and 8 H⁺ are used, but only 6 electrons and 6 H⁺ are theoretically needed to reduce N₂ to 2NH₃. Step 2: The remaining 2e⁻ and 2H⁺ are used to produce one molecule of H₂. Step 3: This means nitrogenase always 'wastes' some electrons by producing H₂, making nitrogen fixation slightly inefficient. Step 4: This is an inherent characteristic of the nitrogenase enzyme — it cannot avoid this hydrogen evolution. Step 5: Options A, C, and D are factually incorrect — H₂ is a byproduct of energy wastage, not a reactant or pH regulator or reduce
Azotobacter is classified as an aerobic, free-living, non-photosynthetic nitrogen-fixing bacterium. How does Azotobacter protect its nitrogenase enzyme from oxygen, given that nitrogenase is oxygen-sensitive?
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Azotobacter has a very high respiration rate that consumes oxygen rapidly, protecting nitrogenase.
Step 1: Nitrogenase enzyme is extremely sensitive to oxygen (O₂) — oxygen inactivates it. Step 2: This creates a paradox for aerobic nitrogen fixers like Azotobacter — they need O₂ for respiration but must keep nitrogenase away from O₂. Step 3: Azotobacter overcomes this by maintaining an extremely high rate of aerobic respiration that rapidly consumes O₂ in its immediate surroundings. Step 4: This creates a locally oxygen-depleted zone around the nitrogenase enzyme. Step 5: Leghemoglobin is found only in legume nodules, not in Azotobacter. Heterocysts are structures found in cyanobacteria lik
In transamination reactions for amino acid synthesis, which of the following pairs correctly identifies the keto acid and the amino acid product when aspartic acid donates its amino group to α-ketoglutaric acid?
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Keto acid product: Oxaloacetic acid; Amino acid product: Glutamic acid
Step 1: In transamination, an amino group (–NH₂) is transferred from an amino acid to a keto acid. Step 2: The reaction is: α-Ketoglutaric acid + Aspartic acid → Glutamic acid + Oxaloacetic acid. Step 3: Aspartic acid (amino acid) donates its amino group to α-ketoglutaric acid (keto acid). Step 4: α-Ketoglutaric acid receives the amino group and becomes Glutamic acid (a new amino acid). Step 5: Aspartic acid, after losing its amino group, becomes Oxaloacetic acid (a keto acid). So the keto acid product is Oxaloacetic acid and the amino acid product is Glutamic acid. Options A, C, and D are inc
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