Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Question
Chapter 18, Problem 10P
Interpretation Introduction
Interpretation:
The reason for, FAD is better electron acceptor than NAD+ in the reaction catalyzed by succinate dehydrogenase.
Concept introduction:
An electron transport chain (ETC) is the series of
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Reductive power. What ratio of NADPH to NADP+ is required to sustain [GSH] = 10 mM and [GSSG] = 1 mM ? Use the redox potentials given in Table 18.1 .
Neep help.
Need help, please.
Chapter 18 Solutions
Biochemistry (Looseleaf)
Ch. 18 - Prob. 1PCh. 18 - Prob. 2PCh. 18 - Prob. 3PCh. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - Prob. 6PCh. 18 - Prob. 7PCh. 18 - Prob. 8PCh. 18 - Prob. 9PCh. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Prob. 14PCh. 18 - Prob. 15PCh. 18 - Prob. 16PCh. 18 - Prob. 17PCh. 18 - Prob. 18PCh. 18 - Prob. 19PCh. 18 - Prob. 20PCh. 18 - Prob. 21PCh. 18 - Prob. 22PCh. 18 - Prob. 23PCh. 18 - Prob. 24PCh. 18 - Prob. 25PCh. 18 - Prob. 26PCh. 18 - Prob. 27PCh. 18 - Prob. 28PCh. 18 - Prob. 29PCh. 18 - Prob. 30PCh. 18 - Prob. 31PCh. 18 - Prob. 32PCh. 18 - Prob. 33PCh. 18 - Prob. 34PCh. 18 - Prob. 35PCh. 18 - Prob. 36PCh. 18 - Prob. 37PCh. 18 - Prob. 38PCh. 18 - Prob. 39PCh. 18 - Prob. 40PCh. 18 - Prob. 41PCh. 18 - Prob. 42PCh. 18 - Prob. 43PCh. 18 - Prob. 44PCh. 18 - Prob. 45PCh. 18 - Prob. 46PCh. 18 - Prob. 47PCh. 18 - Prob. 48PCh. 18 - Prob. 49PCh. 18 - Prob. 50PCh. 18 - Prob. 51PCh. 18 - Prob. 52PCh. 18 - Prob. 53PCh. 18 - Prob. 54PCh. 18 - Prob. 55PCh. 18 - Prob. 56PCh. 18 - Prob. 57PCh. 18 - Prob. 58PCh. 18 - Prob. 59P
Knowledge Booster
Similar questions
- A3arrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forward. Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reactionarrow_forward
- not true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…arrow_forwardAtp bookkeeping. Explain where the number of 38 and 32 atp per glucose molecules comes fromarrow_forwardLong explanations are NOT NEEDED. Answer only d and e. ATP accounting. Consider 1 molecule of the sucrose (monomeric units: glucose and fructose) that will undergo complete oxidation. -Number of pyruvate molecules after glycolysis is 4.-Net ATP produced in glycolysis only (via substrate-level phosphorylation) is 2.-Number of NADH produced using the pyruvate dehydrogenase complex reaction is 1. Now find:d. Number of NADH and FADH2 produced from Krebs cycle.e. Net ATP produced (complete oxidation via Malate aspartate shuttle).arrow_forward
- Small explanation please. what is a product in the first stage of the Q- cycle? a. two electrons b. Q- cation c. cyt c (oxidized) d. two more protons in the matrix e. Q- radical anionarrow_forward. Recall your study of equilibria and kinetics from general chemistry. You used equations with upper case Kand lower case k during the study of equilibria and kinetics respectively. What do the upper and lower case letters refer to?arrow_forward6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?arrow_forward
- Instructions. Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. Name: citryl-CoA synthetase Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA Name: D-xylulose reductase Reaction: xylitol + NAD+ = D-xylulose + NADH + H+ Name: cellobiose phosphorylase Reaction: cellobiose phosphate = α-D-glucose 1-phosphate + D-glucose Name: carbonic anhydrase Reaction: H2CO3 = CO2 + H2O Other info: The enzyme catalyzes the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. Name: pantoate activating enzyme Reaction: ATP + (R)-pantoate = AMP + diphosphate + (R)-pantothenate.arrow_forward7.arrow_forwardSelect the incorrect statement. With regards to free energy ΔG of the reaction below E+S ⇌ ES Negative ΔG mean the reaction toward is facourable More negative value of ΔG indicates stronger binding to S to E It is possible to compute disassociation constant from the ΔG value alone It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone ΔG = 0 indicates (ES)/(E)(S) =1 None of the abovearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning