BIOLOGY
5th Edition
ISBN: 9781265202859
Author: BROOKER
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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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Focusing on the mechanism linking complex I and ATP synthase depicted in figure 3 in the article, compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.
Q177
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
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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- (e) Write 3 assumptions that could be made when using the type of support materials as suggested in (d).arrow_forwardBiochemists 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…arrow_forwardPractice 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 Reactionarrow_forward
- Graph 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_forward10arrow_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
- Question in photoarrow_forward1. 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_forwardSolve the following problems using the basic assumptions: 1 NADH --> 2.5 ATP; 1 FADH2 --> 1.5 ATP Complete degradation of glucose will yield -686 kcal/mol. However, computing the energy yield from 32 ATPs at -7.3 kcal/mole each will only yield -233.6 kcal/mole. What is the percentage yield by the cell? Answer must be whole number.arrow_forward
- To 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_forwardCan you please explain the relationship of ATP concentration and NADH concentration in this graph (cellular respiration)? At different treatments of ATP (E.g. At 25 ATP, 50 ATP, 100 ATP), why did the NADH concentration change?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
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