BIOCHEMISTRY (LL)
9th Edition
ISBN: 9781337805100
Author: Campbell
Publisher: CENGAGE L
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Chapter 6, Problem 2RE
RECALL Are all enzymes proteins?
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fill in the blank and circle the active site for each molecule.
urgent!
fill in the table and circle the active site
The two half reactions
for beginning and end of the electron transport chain are given below in standard form. Calculate & for the overall process. Using the Nernst equation (AG° = -n Fo, F= 96.485 kJ/volt mol), calculate AG°. Explain the need for a stepwise process in the electron transport chain.
NAD* + H+ + 2 e- = NADH
½ 0г + 2H+ + 2е- = H20
= -0.32v
E = +0.82V
Chapter 6 Solutions
BIOCHEMISTRY (LL)
Ch. 6 - RECALL How does the catalytic effectiveness of...Ch. 6 - RECALL Are all enzymes proteins?Ch. 6 - MATHEMATICAL Catalase breaks down hydrogen...Ch. 6 - REFLECT AND APPLY Give two reasons why enzyme...Ch. 6 - RECALL For the reaction of glucose with oxygen to...Ch. 6 - REFLECT AND APPLY Would nature rely on the same...Ch. 6 - REFLECT AND APPLY Suggest a reason why heating a...Ch. 6 - REFLECT AND APPLY A model is proposed to explain...Ch. 6 - REFLECT AND APPLY Does the presence of a catalyst...Ch. 6 - REFLECT AND APPLY What effect does a catalyst have...
Ch. 6 - REFLECT AND APPLY An enzyme catalyzes the...Ch. 6 - REFLECT AND APPLY Can the presence of a catalyst...Ch. 6 - RECALL For the hypothetical reaction 3A+2B2C+3D...Ch. 6 - REFLECT AND APPLY The enzyme lactate dehydrogenase...Ch. 6 - REFLECT AND APPLY Would you use a pH meter to...Ch. 6 - REFLECT AND APPLY Suggest a reason for carrying...Ch. 6 - RECALL Distinguish between the lock-and-key and...Ch. 6 - RECALL Using an energy diagram, show why the...Ch. 6 - REFLECT AND APPLY Other things being equal, what...Ch. 6 - REFLECT AND APPLY Amino acids that are far apart...Ch. 6 - REFLECT AND APPLY If only a few of the amino acid...Ch. 6 - RECALL Show graphically how the reaction velocity...Ch. 6 - RECALL Define steady state, and comment on the...Ch. 6 - RECALL How is the turnover number of an enzyme...Ch. 6 - MATHEMATICAL For an enzyme that displays...Ch. 6 - MATHEMATICAL Determine the values of KM and Vmax...Ch. 6 - MATHEMATICAL The kinetic data in the following...Ch. 6 - MATHEMATICAL The enzyme -methylaspartase catalyzes...Ch. 6 - MATHEMATICAL The hydrolysis of a...Ch. 6 - MATHEMATICAL For the Vmax obtained in Question 26,...Ch. 6 - MATHEMATICAL You do an enzyme kinetic experiment...Ch. 6 - REFLECT AND APPLY The enzyme D-amino acid oxidase...Ch. 6 - REFLECT AND APPLY Why is it useful to plot rate...Ch. 6 - REFLECT AND APPLY Under what conditions can we...Ch. 6 - BIOCHEMICAL CONNECTIONS Why does acetazolamide...Ch. 6 - BIOCHEMICAL CONNECTIONS How did scientists...Ch. 6 - BIOCHEMICAL CONNECTIONS How do the KM values for...Ch. 6 - Prob. 38RECh. 6 - RECALL What are the three most common mechanisms...Ch. 6 - RECALL What is the biggest difference between a...Ch. 6 - RECALL How do scientists determine the KM of a...Ch. 6 - Prob. 42RECh. 6 - Prob. 43RECh. 6 - RECALL Do all enzymes display kinetics that obey...Ch. 6 - RECALL How can you recognize an enzyme that does...Ch. 6 - RECALL If we describe an enzyme like aspartate...Ch. 6 - RECALL How can competitive and pure noncompetitive...Ch. 6 - RECALL Why does a competitive inhibitor not change...Ch. 6 - RECALL Why does a pure noncompetitive inhibitor...Ch. 6 - RECALL Distinguish between the molecular...Ch. 6 - RECALL Can enzyme inhibition be reversed in all...Ch. 6 - RECALL Why is a Lineweaver-Burk plot useful in...Ch. 6 - RECALL Where do lines intersect on a...Ch. 6 - RECALL What is the difference between pure and...Ch. 6 - REFLECT AND APPLY Why can we say that having a...Ch. 6 - REFLECT AND APPLY When we compare the binding of I...Ch. 6 - RECALL Why does the apparent KM decrease in the...Ch. 6 - RECALL What is a suicide substrate? Why are they...Ch. 6 - RECALL If we made a Lineweaver-Burk plot of an...Ch. 6 - Prob. 60RECh. 6 - MATHEMATICAL For the following aspartase reaction...Ch. 6 - REFLECT AND APPLY Is it good (or bad) that enzymes...Ch. 6 - REFLECT AND APPLY Noncompetitive inhibition is a...Ch. 6 - BIOCHEMICAL CONNECTIONS You have been hired by a...Ch. 6 - REFLECT AND APPLY Would you expect an irreversible...Ch. 6 - REFLECT AND APPLY Would you expect the structure...Ch. 6 - Prob. 67RECh. 6 - Prob. 68RE
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- answer the questions and the example steps should be from carbohydrates glycolysis and citric acid cycle. Please put down reactions and structuresarrow_forwardidentify the general type of reaction catalyzed and an example step from glycolisis structure for each of the following enzymes/ co factor Kinase, isomerase, mutase, dehydrogenase, NAD+ , FADarrow_forwardfill in the blanks with the missing structures and give namesarrow_forward
- fill in the table and identify the general type of reaction catalayzed and an example step from the structures in the second page so you will answer the questions from the first page the second one is just a reference urgently!arrow_forwardPlease draw out the molecular structures of each molecule and show how each enzyme + cofactor would affect the following molecule in the human metabolic pathway. (This is a metabolic map)arrow_forwardPlease draw out the molecular structures of each molecule and show how an enzyme + cofactor would affect the following molecule in the human metabolic pathway to create energy.arrow_forward
- Please draw out the molecular structures of each molecule and show how each enzyme + cofactor would affect the following molecule in the human metabolic pathway.arrow_forwardPlease draw out the mechanism with curved arrows showing electron flow. Pyruvate is accepted into the TCA cycle by a “feeder” reaction using the pyruvate dehydrogenase complex, resulting in acetyl-CoA and CO2. Provide the mechanism for this reaction utilizing the TPP cofactor. Include the roles of all cofactors.arrow_forwardPyruvate is accepted into the TCA cycle by a “feeder” reaction using the pyruvate dehydrogenase complex, resulting in acetyl-CoA and CO2. Provide the mechanism for this reaction utilizing the TPP cofactor. Include the roles of all cofactors.arrow_forward
- The mitochondrial ATP synthase has 10 copies of the F0 subunit “c”, and the [H ] in the mitochondrial inner membrane space (IMS) is 6.31 x 10-8 M and the [H + ] in the matrix is 3.16 x 10-9 M. Calculate the minimum membrane potential (∆Ψ) necessary to make ATP synthesis thermodynamically favorable. [Assume ∆G' ofphosphate hydrolysis of ATP is - 45 kJ/mol.]arrow_forwardB- Vitamins are converted readily into important metabolic cofactors. Deficiency in any one of them has serious side effects. a. The disease beriberi results from a vitamin B 1 (Thiamine) deficiency and is characterized by cardiac and neurological symptoms. One key diagnostic for this disease is an increased level of pyruvate and α-ketoglutarate in the bloodstream. How does this vitamin deficiency lead to increased serumlevels of these factors? b. What would you expect the effect on the TCA intermediates for a patient suffering from vitamin B 5 deficiency? c. What would you expect the effect on the TCA intermediates for a patientsuffering from vitamin B 2 /B 3 deficiency?arrow_forwardPyruvate is accepted into the TCA cycle by a “feeder” reaction using the pyruvate dehydrogenase complex, resulting in acetyl-CoA and CO2. Provide a full mechanism for this reaction utilizing the TPP cofactor. Include the roles of all cofactors.arrow_forward
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