The nitrogenase complex can reduce molecules other than N2. Provide the structures for the products for each of the following substrates (real and hypothetical) that contain triple bonds: hydrogen cyanide, dinitrogen, and acetylene.

The nitrogenase complex can reduce molecules other than N2. Provide the structures for the products for each of the following substrates (real and hypothetical) that contain triple bonds: hydrogen cyanide, dinitrogen, and acetylene.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter22: Gluconeogenesis, Glycogen Metabolism, And The Pentose Phosphate Pathway

Section: Chapter Questions

Problem 23P: Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the...

See similar textbooks

Related questions

Q: Identify the biochemical advantages that the glyoxylate cycle provides.

A: The glyoxylate cycle bypasses the decarboxylation steps of the citric acid cycle. where the…

Q: Isomerization of the following ketose can give two aldoses. Draw the structures of the two aldoses…

A: The given sugar is α-D-fructose. α-D-fructose is a ketose sugar. Carbohydrates or sugar molecules…

Q: There are two competing processes for the manufacture of lactic acid, chemical and biochemical…

A: Lactic acid is an organic compound, its Chemical name is 2-hydroxypropanoic acid and belongs to…

Q: The mechanism involved in the reaction catalyzed by phosphoglyceromutase is known to involve a…

A: Glycolysis is breakdown of glucose to provide energy. Phosphoglyceromutase catalyze the conversion…

Q: H2N H -N Orcinol но Δ а. но он a.

A: The shown molecule is guanosine which is a purine molecule and it is here in the given reaction is…

Q: There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for…

A: Cysteine proteases are proteases that degrade protein and are also called thiol proteases. They use…

Q: Examination of the cleavage of the amide substrate, A, by chymotrypsin with the use of stopped-flow…

A: Proteolytic enzymes commonly known as proteases are used for the cleavage of protein. Chymotrypsin…

Q: Glutamate dehydrogenase functions to produce ammonia for the urea cycle. Use the standard reduction…

A: Glutamate dehydrogenase is the enzyme that is responsible for the production of ammonia. Ammonia…

Q: Some diazotrophs produce a vanadium-containing VFe protein in addition to the MoFe protein. The…

A: A group of enzymes that can fix atmospheric nitrogen into ammonia is collectively known as…

Q: Propose a metabolic I pathway for methotrexate

A: Methotrexate and its active polyglutamate metabolites interfere with several intracellular metabolic…

Q: A reaction involved in the metabolism of sugars is the splitting of fructose-1,6-diphosphate to give…

A: Glycolysis is the process by which one molecule of glucose is converted into two molecules of…

Q: Seduheptulose is an intermediate in respiratory and photosynthetic pathways and plays a vital role…

A: a. The stable form of sugars like pentose and hexose sugars are five or six-atom rings and these…

Q: Describe the application of transamination in the biosynthesis of shikimate derivatives. Show how…

A: Shikimic is derived from the Japanese flower shikimi (Japanese star anise, Illicium anisatum), from…

Q: The metabolism of alcohol pathway is showed in the figure characterized by biotransformation of:…

A: Metabolism- The primary enzyme involved in the metabolism of alcohol is ADH( Alcohol dehydrogenase)…

Q: Considering the general structure of penicillins, how are they rendered ineffective? Select…

A: Penicillin is an antibiotic that inhibits the formation of peptidoglycan cross-links of the…

Q: Describe the mechanism of a-chymotrypsin. Explain the roles of constituents of the catalytic triad,…

A: Chymotrypsin is a enzyme secreted by the pancrease and poured into the duodenum of the small…

Q: [methyl-14C]Pyruvate was administered to isolated liver cells in the presence of sufficient malonate…

A: Succinate dehydrogenase or respiratory complex II is an enzyme complex, found in many bacterial…

Q: Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the…

A: Answer i- A catalytic triad is a group of three amino acids present in the active site of some…

Q: One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation…

A: Lead act as poison by binding to different enzymes. Lead is soluble in water when it is present in…

Q: Ethyl alcohol is sometimes used in hospital emergency rooms to treat patients who have ingested…

A: The main components of the antifreeze are methanol, glycerol, ethylene glycol, and propylene glycol.…

Q: Consider the dextran sucrase reaction. Why do you suppose there is not an ATP requirement to…

A: Dextran sucrase is an enzyme that catalyses the chemical reaction.

Q: Looking at the structure of RDV-TP, what changes in the structure of the molecule does the active…

A: The building blocks of DNA and RNA are purine and pyrimidin. Purine are heterocyclic compound.…

Q: Given each set of information which may include common name(s) and the reaction catalyzed, you are…

A: Note : Hi ! Thank you for the question. We are authorized to answer three subparts at a time. Since…

Q: How many tritium atoms (3H) are incorporated into palmitate when fattyacid synthesis is carried out…

A: Palmitate synthesis requires the input of 8 acetyl CoA molecules, 14 NADPH molecules and 7 ATPs.…

Q: Some archaebacteria produce an enzyme with two active sites: one catalyzes the dephosphorylation of…

A: Archaebacteria contains an enzyme Fructose-1,6-bisphosphate aldolase which is a bifunctional enzyme…

Q: The reagent periodate (IO, ) oxidatively cleaves the carbon-carbon bonds between two carbons…

A: Metabolically plants and animals are different in several metabolic stages, plants have ability to…

Q: In addition to cleaving peplides, chymotrypsin can akso catalyze the hydrołysis of certain small…

A: Hi! Thank you for the question. We are authorized to answer one question at a time, since you have…

Q: Given each set of information which may include common name(s) and the reaction catalyzed, you are…

A: Enzymes have a common name that provides little information about the reaction catalyzed by…

Q: Behenate (C22H44O2) can be obtained by chain elongation from palmitate. How many ATP equivalents are…

A: Introduction;- Adenosine 5′-triphosphate, abbreviated as ATP and generally written without the 5′-,…

Q: If you were to determine the P/O ratio for oxidation of a-ketoglu- tarate, you would probably…

A: During the oxidation of α-ketoglutarate, some malonate may be added to block succinate…

Q: Consider applying biocatalytic reduction with carrots to the following two ketones: tert-butyl…

A: Introduction :- Bio-catalysis is the process of using natural substances like- enzymes for…

Q: The isoelectric point (pI) of 6-phosphogluconate dehydrogenase is 6.0. Explain why the buffer used…

A: Enzymes are a class of proteins except for ribozymes (class of RNA) that elevates the pace of the…

Q: Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to…

A: Henderson-Hasselbalch equation relates pH, pKa and the ratio of concentrations of protonated to…

Q: An L-amino acid oxidase in mammalian peroxisomes requires H2O and O2 as substrates and catalyzes…

A: L-amino acid oxidase are flavoenzymes.

Q: Determine whether the following reactions will be spontaneous under standard biochemical conditions.…

A: An exergonic reaction is one in which the energy level of the products is lower than the energy…

Q: Identify each of the following biomolecules. Explain the function of each in biochemical processes.…

A: Biomolecules are macromolecules that are composed of carbon, hydrogen, oxygen, and nitrogen…

Q: Normal carbonic anhydrase has zinc at its active site . Suggest a structural reason why…

A: Almost all organisms contain enzymes, carbonic anhydrases, that catalyze CO2 hydration and…

Q: Serine esterase contains a catalytic triad at its active site. Which amino acid in serine esterase…

A: Serine esterase contains three amino acids, His 57,Ser 195 and Asp 102.These three residues form a…

Q: [methyl-14C]Pyruvate was administered to isolated liver cells in the presence of sufficient malonate…

A: When the radioactive pyruvate at methyl carbon (carbon number 3) would be administered to the liver…

Q: this drug contains one or more building blocks derived from either ethylene oxide or…

A: Drugs are the chemical agents used to treat disease and other ailments. Drugs can be naturally…

Q: In order to function as an oxidative phosphorylation uncoupler (page 648), 2,4-dinitrophenol must…

A: Uncouplers such as DNP decreases the formation of high energy phosphate and stimulate oxygen…

Q: The four-carbon sugar erythrose-4-phosphate is the starting material in the synthesis of many…

A: Erythrose 4 phosphate is a phosphate of erythrose. Erythrose 4 phosphate is an intermediate compound…

Q: Given the following substrates and enzymes, provide a Scheme to the tri-deuterated 5,10-…

A: A. Sulfotransferase- This name is made by combining two words - sulfo + transferase. It suggests…

Q: Malonate competes with succinate in the succinate dehydrogenase reaction. Explain why increasing the…

A: Enzymatic inhibitors decrease enzyme activity. Where the enzyme inhibition is of 3 types…

Q: Methyl amines are often demethylated by cytochrome P450 enzymes. Propose a mechanism for the…

A: Methylamines, like monomethylamine (MMA), Dimethylamine (DMA), and Trimethylamine (TMA) are the…

Q: Write balanced equations for the three known reactions that transfer anamino group to a substrate by…

A: IMP (Inosine monophosphate) synthesis (purine synthesis): - the 7th step in this process include…

Q: In some brain cancer cells, a mutated form of isocitrate dehydrogenase, instead of catalyzing the…

A: The brain is part of the central nervous system. It is located inside the skull. The brain has three…

Q: The purinosome contains enzymes that convert the serine hydroxymethyl group to the formyl group of…

A: Purinosome refers to a multi-enzyme complex, which is involved in carrying out the purine…

Q: Carboxylic acids

A: carboxylic acids are more difficult to reduce than aldehydes and ketones, there are some agents…

Q: Write out the balanced chemical equation for the FIRST round of oxidation of C16:cis-9.

A: in the first round of beta oxidation, we will have a 2C short acyl Co A, an acetyl Co A, FADH2 and…

Q: There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase?…

A: Malate dehydrogenase catalyzes the reversible conversion of malate into oxaloacetate. This is the…

Concept explainers

Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.

Question

The nitrogenase complex can reduce molecules other than N2. Provide the structures for the
products for each of the following substrates (real and hypothetical) that contain triple bonds:
hydrogen cyanide, dinitrogen, and acetylene.

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.

Similar questions

Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.
Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
An inhibitor that specifically labels chymotrypsin at histidine 57 is Ntosylamido-l-phenylethyl chloromethyl ketone. How would you modify the structure of this inhibitor to label the active site of trypsin?
How many tritium atoms (3H) are incorporated into palmitate when fattyacid synthesis is carried out in vitro with the following labeled substrate?
An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl chloromethylketone. How would you modify the structure of this inhibitor tolabel the active site of trypsin?
In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?
Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)
In order to function as an oxidative phosphorylation uncoupler, 2,4-dinitrophenol must act catalytically, not stoichiometrically. What does this mean? Identify and discuss an important implication of this conclusion.
There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
Considering the general structure of penicillins, how are they rendered ineffective? Select one: a. β-Lactamase performs nucleophilic attack of the amide in the penicillin side chain b. β-Lactamase performs nucleophilic attack of the amide in the β-lactam ring and subsequently hydrolyzes this intermediate c. β-Lactamase performs nucleophilic attack of the thiazolidone ring on the carbon next to the electronegative sulfur leading to a covalently inhibited β-Lactamase d. All of these e. None of these
The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?