Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 7.6, Problem 1EQ
Summary Introduction
To predict: The way in which the movement of ATP synthase was observed by researchers.
Introduction: With the help of the enzyme, ATP synthase, ATP occurs in cells. It combines an inorganic phosphate molecule with ADP. An experiment was conducted to observe the ATP synthase molecule. The components of the molecule were observed to be too small to be visualized by a light microscope.
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Biochemists working with isolated mitochondria recognize five
energy "states" of mitochondria, depending on the presence or
absence of essential substrates for respiration-O, ADP, oxidizable
substrates, and so forth. The characteristics of each state are:
state 1: mitochondria alone (in buffer containing P;)
state 2: mitochondria + substrate, but respiration low due to
lack of ADP
Practice
Mira Gendy
1 of 1
Directions: This short free-response question requires about 6 minutes to answer. The question is worth 3 points. Read the question carefully and completely. Answers must be written
out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable.
II
Substrate Concentration [S]
The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the presence of a constant concentration of the enzyme.
Connect the primary structure of the enzyme to its overall shape.
I U
x X2 5
Initial Rate of Reaction
Biochemists working with isolated mitochondria recognize five energy“states” of mitochondria, depending on the presence or absence of essential substrates for respiration—O2, ADP, oxidizable substrates, and so forth. The characteristics of each state are:state 1: mitochondria alone (in buffer containing Pi)state 2: mitochondria + substrate, but respiration low due to lack of ADPstate 3: mitochondria + substrate + limited amount of ADP, allowingrapid respirationstate 4: mitochondria + substrate, but all ADP converted to ATP, sorespiration slowsstate 5: mitochondria + substrate + ADP, but all O2 used up (anoxia),so respiration stops(a) On the graph, identify the state that might predominate in each stage of the trace indicated with a letter. (b) To determine whether isolated mitochondria exhibit respiratory control,one determines the ratio of rates of oxygen uptake in two different states.Which states?(c) Which state probably predominates in vivo in skeletal muscle fatiguedfrom a long…
Chapter 7 Solutions
Biology
Ch. 7.2 - Core Skill: Connections Look ahead to Table 45.1....Ch. 7.2 - Which organic molecules donate a phosphate group...Ch. 7.2 - Prob. 2CSCh. 7.4 - Prob. 1CCCh. 7.5 - Explain the meaning of the name cytochrome...Ch. 7.6 - Prob. 1CCCh. 7.6 - Prob. 1CSCh. 7.6 - Prob. 1EQCh. 7.6 - CoreSKILL In the experiment of Figure 7.13, what...Ch. 7.6 - Prob. 3EQ
Ch. 7.7 - Prob. 1CCCh. 7 - Which of the following pathways occurs in the...Ch. 7 - Prob. 2TYCh. 7 - Prob. 3TYCh. 7 - Which organic molecule supplies a two-carbon group...Ch. 7 - The ability to diagnose tumors using...Ch. 7 - Prob. 6TYCh. 7 - Certain drugs, which are called ionophores, cause...Ch. 7 - Prob. 8TYCh. 7 - Prob. 9TYCh. 7 - Prob. 10TYCh. 7 - Prob. 1CQCh. 7 - What causes the rotation of the subunit of ATP...Ch. 7 - Core Concept: Energy and Matter How is glucose...Ch. 7 - Discuss the advantages and disadvantages of...Ch. 7 - Prob. 2COQ
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- Image shows reaction for hydrogen ion transport from outside mitochondrion to inside mitochondrion. Part a) What is ∆G ̊ for hydrogen ion transport. Part b) Outside the mitochondria there is a pH of 6.4 and inside mitochondria, there is a pH of 7.4. Calculate Q and ∆G for the reaction shown in the image. Part c) How many hydrogen ions needed per one ATP?arrow_forwardGraph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ? Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.arrow_forwardAn enzyme with a Km of 3 X 10-4 M was tested at an initial substrate concentration of 10-5 M. In 1 minute, 5% of the substrate was found to be utilized. (a) What percentage of the substrate was utilized in 5 minutes? (b) If the initial substrate concentration had been 8 X 10-7 M, what percentage of the substrate would have been utilized in 5 minutes? (c) Vmax =? (d) How long would it take to utilize 50% of the substrate at 8 X 10-7 M? (e) How long would it take to utilize 75% of the substrate at 10-5 M?arrow_forward
- 1. a) Describe what is happening in ATP Synthase in plain English! (how would you describe this step for someone who hasn’t taken Biol) b) If someone wanted to perform an experiment to evaluate the output of a particular step, which variable would be the best option to measure? (Think about which variable is UNIQUE to each step!)arrow_forwardTo examine: Whether the statement, “The number of c subunits in the rotor ring of ATP synthase defines how many protons need to pass through the turbine to make each molecule of ATP." is true or false.arrow_forwardExercise The following data describe an enzyme-catalyzed reaction. Plot these results using the Lineweaver-Burk method, and determine values for KM and Vinax- The symbol mM represents millimoles per liter; 1 mM = 1 × 10 3 mol L. (The concentration of the enzyme is the same in all experiments.) Velocity (mM sec-") Substrate Concentration (тм) 2.5 0.024 5.0 0.036 10.0 0.053 15.0 0.060 20.0 0.061 Ippt.comarrow_forward
- Suppose the concentration of glucose inside a cell is 0.1 mM and the cell issuspended in a glucose solution of 0.01 mM.(a) What would be the free energy change, in kJ/mol, for the transport ofglucose from the medium into the cell? Assume T = 37 °C.(b) What would be the free energy change, in kJ/mol, for the transport ofglucose from the medium into the cell if the intracellular and extracellularconcentrations were 1 mM and 10 mM, respectively?(c) If the processes described in parts (a) and (b) were coupled toATP hydrolysis, how many moles of ATP would have to be hydrolysed,per mole of glucose transported, in order to make each process favorable? (Use the standard free energy change for ATP hydrolysis.)arrow_forwardJ. C. Servaites, in Plant Physiol. (1985) 78:839–843, observed that Rubisco from tobacco leaves collected before dawn had a much lower specific activity than the enzyme collected at noon. This difference persisted despite extensive dialysis, gel filtration, or heat treatment. However, precipitation of the predawn enzyme by 50% (NH4)2SO4 restored the specific activity to the level of the noon-collected enzyme. Suggest an explanation.arrow_forwardWhy does growth of ETPUM in Medium # require oxygen? ' ink about this in terms of howETPUM can generate a net gain in ATP by processing polyurethane. Remember that the degradationof polyurethane by polyurethanase does not expend ATP. In order to answer this question, address eachof the following questions in your answer:a. Is there a net gain or loss of ATP during the transport of the citrate?b. Consider the ATPs that can be generated via substrate-level phosphorylation. Will glycolysis beuseful for generating any ATPs during growth on polyurethane? How many ATPs can be generatedvia TCA? Is this enough to support growth (is there a net positive in the ATP tally)?c. Now consider how else ETPUM can generate ATPs (if not by substrate- level phosphorylation). Canthis process generate a net positive in the ATP tally?d. Now explain the importance of oxygen as relates to the ATP tally.arrow_forward
- 2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…arrow_forwardWe have discussed the aerobic metabolism of glucose extensively in this class. To capture and use the energy in glucose to make ATP, we must utilize 4 different sequential pathways/steps. Starting with one glucose molecule and eventually ending with CO, H;O and ATP, list the 4 pathways/steps in order and tell me what molecules enter each pathway, and what the final products of each pathway are. Edit View Insert Format Tools Table 12pt v Paragraph v BIUAv ev Tov : Iarrow_forwardNa-K" ATPase ATP + H₂O 2 K+ ADP + P₁ Na Na OD) K Na Na K Na Na Na "K" Na E) a, b, and c C) A symporter K a and b only Na Na Na Glucose Na Na Glucose Na Glucose The diagram below describes: SGLT Glucose A) How the pumping of sodium ions out of the cell can power the transport of glucose into the cell. B) Two types of active transport Na Na Na K"arrow_forward
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