+Draw the missing organic structures in the followingmultistep synthesis. Show the final product atphysiological pH (pH = 7.4). Ignore any inorganicbyproducts formed.HNO1. NaOCH2CH32. CH3ISelect to DrawQ

Step 1: Step 2: Step 3: Step 4:

Answered: + Draw the missing organic structures…

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter23: Enzymes

Section: Chapter Questions

Problem 23.9P

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Consider the following biochemical reactions: H₂N-CH-C-NH-CH-C- CH3 _________ reaction A B с HO-CH2 H HO -OH H OH H H OH OH + H₂O ATP ADP enzyme 0 0 0 NADH enzyme enzyme type of enzyme needed to catalyze this reaction HỎ 2 H₂N- CH₂ NAD La pl OH -O, H он н ¸ÑLÒ¯ CH₂ H OH In the table below, write the type of enzyme that catalyzes each reaction. Note: be sure to use only the 6 standard enzyme types. OH A B с
AH = - 1.2 kcal/mol; Kp = 16 nM OH 1 HO AH = - 6.0 kcal/mol; N. Kp = = 76 nM OH 2 HOl. AH = - 5.5 kcal/mol; Kp = 0.5 nM OH (iii) By considering the enthalpies given, what do you think this suggests about the target (e.g. the binding pocket of an enzyme) that the molecule binds to?
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For a given acid HA, it was determined that at pH 6.0 the concentration of the conjugate base [A] was 0.075 M and the acid [HA] was 0.025 M. What percent of this acid is ionized at pH 6.0? What is the pKa of this acid? What pH would this acid be 50% lonized?
. Opposites attract. The following graph shows how the AGAG for the hydrolysis of ATP varies as a function of the Mg2+Mg*+ concentration (pMg=-log[ Mg2+ ]).(pMg = –log [Mg²+]). 36 8.6 8.4 35 8.2 34 8.0 을 33 7.8 7.6 7.4 31 7.2 30 1 2 3 4 5 6 7 pMg Berg et al., Biochemistry, 9e, © 2019 W. H. Freeman and Company a. How does decreasing [ Mg2+ ]lMg*"] affect the AGAG of hydrolysis for ATP? b. Explain this effect. -AG (kJ mol-1) -AG (kcal mol-)
The second step in the catabolism of most amino acids is the removal of the nitrogen atom from glutamate by oxidative deamination. In this reaction, glutamate is converted to an a-keto acid. Modify the structure to show the a-keto acid product. ?- || с I CH₂ I H₂N- & + remaining products enzyme CH₂ I CH₂ + NAD+ + H₂O CH₂ Incorrect Enter the chemical formulas for the remaining products. remaining products: NADH + H+ + NH Identify the enzyme that catalyzes the reaction. The enzyme that catalyzes the reaction is glutamate dehydrogenase. OH OH
9. Give the reactions of the oxidative deamination for glutamic acid (E). Show all the structures of the compounds involved; indicate whether the reactions are reversible or not; show the use or generation of co-factors wherever it occurs. 2p H₂ HOOC COOH 2 C H₂ C- CH NH3*
Indicar los productos (y su estereoquímica) y el tipo de mecanismo Ph (razonado). H3CC CH3CH₂ -Br H₂O
Chemistry 3.Calculate the amount of free energy required (or released) to allow electron transport in the ETC to be spontaneous from NADH to ubiquinone under standard conditions based on two electrons moving through the system. This occurs at 25°C. ½ O2 + 2e + 2H+ ® H2O E°´ = 0.815 V NAD+ + 2e +H+ ® NADH E°´ = -0.315 V NADP+ + H+ + 2e ® NADPH E°´ = -0.320 V FAD + 2e +2H+ ® FADH2 E°´ = -0.219 V Ubiquinone + 2H + 2e ® Ubiquinol E°´ = 0.045 V
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+ Draw the missing organic structures in the following multistep synthesis. Show the final product at physiological pH (pH = 7.4). Ignore any inorganic byproducts formed. HN O 1. NaOCH2CH3 2. CH3I Select to Draw Q