BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
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Chapter 18, Problem 9P
Interpretation Introduction
Interpretation:
The free energy required by FADH2 to reduce O2.
Concept introduction:
The redox potential is the measure of tendency of any chemical compound to lose or accept electrons and attain an oxidized or reduced state. The electrode potential of a compound to accept an electron is termed as reduction potential. Further, the oxidation potential is the potential of the compound on losing its electrons.
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Examine the metabolic pathway. The enzymes that catalyze each step are identified as "e" with a numeric subscript.
e₁
e3
e4
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e5
e6
e7
E
F
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e
ez
☐ ez
e4
☐
ப
es
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ез
e4
es
26
5
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An allosteric enzyme that follows the concerted model has an allosteric coefficient (T/R) of 300 in the absence of substrate.
Suppose that a mutation reversed the ratio.
Select the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate
concentration, [S].
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The enzyme would likely follow Michaelis-Menten kinetics.
The plot of V versus [S] would be sigmoidal.
The enzyme would mostly be in the T form.
The plot of V versus [S] would be hyperbolic.
The enzyme would be more active.
Penicillin is hydrolyzed and thereby rendered inactive by penicillinase (also
known as ẞ-lactamase), an enzyme present in some penicillin-resistant
bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kDa.
The amount of penicillin hydrolyzed in 1 minute in a 10.0 mL. solution
containing 1.00 x 10 g of purified penicillinase was measured as a
function of the concentration of penicillin. Assume that the concentration of
penicillin does not change appreciably during the assay.
Plots of V versus [S] and 1/V versus 1/[S] for these data are shown.
Vo (* 10 M minute"¹)
7.0
6.0
5.0
4.0
3.0
20
1.0
0.0
о
10
20
30
1/Vo (* 10 M1 minute)
20
103
90
BO
70
50
[S] (* 100 M)
40
50
60
y=762x+1.46 × 10"
[Penicillin] (M)
Amount hydrolyzed (uM)
1
0.11
3
0.25
5
0.34
10
0.45
30
0.58
50
0.61
Chapter 18 Solutions
BIOCHEMISTRY
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
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