2. In contrast to the toxicity of 2-fluoro-citrate, L-(2-fluoro-)succinate is not an inhibitor of succinate dehydrogenase and the product 2-fluoro-fumarate is converted by fumarate hydratase to L-(2-fluoro-2- hydroxy)malate that breaks down to oxaloacetate. Does the oxidation of 2-fluoro-succinate yield the same number of reducing equivalents to (a) the FAD coenzyme of succinate dehydrogenase as the normal substrate? Write the reaction with structural formulas to illustrate your answer. 2-fluoro-fumarate is a substrate of fumarate hydratase forming only L-(2-fluoro-2-hy- (b) droxy)malate, which breaks down spontaneously to oxaloacetate. Write the equation with structural formulas. Oxaloacetate has been shown to be a very po- (c) tent inhibitor of succinate dehydrogenase. For the enzyme isolated from cardiac muscle the Kj value is ~4 x 10-6M, as shown in the L-B plot on the right. Yet, this inhibition is never discussed in biochemistry textbooks. From your reading in the textbook, suggest two reasons why this in- hibition may not be metabolically consequential in the mi- tochondrion. 0.5 1.0 1.5 2.0 Buccinate (mM) Inhibition of succinate dehydrogenase by oxalo- acetate. O, no oxaloacetate; A, 5.4 µM ox- aloacetate; ●, 10.8 µM oxaloacetate. 1(umole"!min.mg protein)
2. In contrast to the toxicity of 2-fluoro-citrate, L-(2-fluoro-)succinate is not an inhibitor of succinate dehydrogenase and the product 2-fluoro-fumarate is converted by fumarate hydratase to L-(2-fluoro-2- hydroxy)malate that breaks down to oxaloacetate. Does the oxidation of 2-fluoro-succinate yield the same number of reducing equivalents to (a) the FAD coenzyme of succinate dehydrogenase as the normal substrate? Write the reaction with structural formulas to illustrate your answer. 2-fluoro-fumarate is a substrate of fumarate hydratase forming only L-(2-fluoro-2-hy- (b) droxy)malate, which breaks down spontaneously to oxaloacetate. Write the equation with structural formulas. Oxaloacetate has been shown to be a very po- (c) tent inhibitor of succinate dehydrogenase. For the enzyme isolated from cardiac muscle the Kj value is ~4 x 10-6M, as shown in the L-B plot on the right. Yet, this inhibition is never discussed in biochemistry textbooks. From your reading in the textbook, suggest two reasons why this in- hibition may not be metabolically consequential in the mi- tochondrion. 0.5 1.0 1.5 2.0 Buccinate (mM) Inhibition of succinate dehydrogenase by oxalo- acetate. O, no oxaloacetate; A, 5.4 µM ox- aloacetate; ●, 10.8 µM oxaloacetate. 1(umole"!min.mg protein)
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Question
Transcribed Image Text:2. In contrast to the toxicity of 2-fluoro-citrate, L-(2-fluoro-)succinate is not an inhibitor of succinate
dehydrogenase and the product 2-fluoro-fumarate is converted by fumarate hydratase to L-(2-fluoro-2-
hydroxy)malate that breaks down to oxaloacetate.
(a)
the FAD coenzyme of succinate dehydrogenase as the normal substrate? Write the reaction with
structural formulas to illustrate your answer.
Does the oxidation of 2-fluoro-succinate yield the same number of reducing equivalents to
(b)
droxy)malate, which breaks down spontaneously to oxaloacetate. Write the equation with structural
formulas.
2-fluoro-fumarate is a substrate of fumarate hydratase forming only L-(2-fluoro-2-hy-
Oxaloacetate has been shown to be a very po-
(c)
tent inhibitor of succinate dehydrogenase. For the enzyme
3
isolated from cardiac muscle the Kj value is ~4 x 10-6M, as
shown in the L-B plot on the right. Yet, this inhibition is
never discussed in biochemistry textbooks. From your
reading in the textbook, suggest two reasons why this in-
hibition may not be metabolically consequential in the mi-
tochondrion.
0.5
1.0
1.5
2.0
succinata (mM)-1
Inhibition of succinate dehydrogenase by oxalo-
acetate. O, no oxaloacetate; A, 5.4 µM ox-
aloacetate;
10.8 µM oxaloacetate.
L (pmole!min.mg protein)
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