Biochemistry 410/411 Textbook - 5th Edition - Custom Texas A&M University
5th Edition
ISBN: 9781119302940
Author: Voet
Publisher: WILEY C
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 18, Problem 14E
Summary Introduction
To calculate: The number of ATP that could be synthesized by the oxidation of acetate by S under standard conditions.
Concept introduction: ATP, the source of energy is gained by the oxidative phosphorylation and electron transport chain in mitochondria. In prokaryotes, ATP is produced in a fashion similar for eukaryotes. The difference is that all the complexes of electron transport chain are present on the cell membrane of the bacteria.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Biochemistry Question.
Please help solve. Thank you!
Based upon knowledge of oxidation of bioorganic compounds and howmuch energy is released during their oxidation, rank the following, from most to least, with respect to how much energy would be produced from each during their oxidation. Explain your placement for each one.
Biochemistry Question.For the metabolism of amino acids what is the first step for theirbreakdown?
Why is it necessary for this breakdown product to be transported to the liver?
For the catabolism of the carbon backbone of these amino acids, there are 7 entry points into the “standard” metabolic pathways. List these 7 entry points and which amino acids are metabolized to these entry points.
Please help. Thank you!
Biochemistry Question. Please help. Thank you.
You are studying pyruvate utilization in mammals for ATP production under
aerobic conditions and have synthesized pyruvate with Carbon #1 labelled with radioactive C14.
After only one complete cycle of the TCA cycle, which of the TCA cycle intermediates would be
labeled with C14? Explain your answer.
Interestingly, you find C14 being excreted in the urine. How does it get there?
Chapter 18 Solutions
Biochemistry 410/411 Textbook - 5th Edition - Custom Texas A&M University
Ch. 18 - Prob. 1ECh. 18 - 2. Certain genetic diseases caused by defective...Ch. 18 - 3. How many ATPs are synthesized for every...Ch. 18 - 4. How many ATPs are synthesized for every...Ch. 18 - 5. Explain why defects in mitochondrial genes...Ch. 18 - 6. Deficiencies of the components of Complexes I,...Ch. 18 - 7. Calculate ?G°+ for the oxidation of free FADH2...Ch. 18 - 8. Show that the free energy change for the...Ch. 18 - Prob. 9ECh. 18 - Prob. 10E
Ch. 18 - Prob. 11ECh. 18 - 12. Under certain conditions, cytochrome c can...Ch. 18 - 13. Some anaerobic prokaryotes use nitrate (NO3?)...Ch. 18 - 14. Some anaerobic prokaryotes reduce elemental...Ch. 18 - Prob. 15ECh. 18 - Prob. 16ECh. 18 - 17. Bombarding a suspension of mitochondria with...Ch. 18 - 18. For the experimental system described in...Ch. 18 - 19. Consider the mitochondrial ADP-ATP...Ch. 18 - 20. What thermodynamic force drives the transport...Ch. 18 - Prob. 21ECh. 18 - Prob. 22ECh. 18 - 23. Explain why compounds such as DNP increase...Ch. 18 - 24. What is the advantage of hormones activating a...Ch. 18 - 25. Describe the changes in [NADH]/[NAD+] and...Ch. 18 - 26. During cell signaling events that increase...Ch. 18 - 27. Activated neutrophils and macrophages (types...Ch. 18 - 28. Mutations in SOD arc associated with the...Ch. 18 - Prob. 29CQCh. 18 - 30. Sketch the O2-consuntption curves obtained for...Ch. 18 - Prob. 31CQCh. 18 - 32. For the mitochondrial membrane described in...Ch. 18 - 33. Nicotinamide nucleotide transhydrogenase (NNT)...Ch. 18 - 34. The antidiabetes drug metformin inhibits...Ch. 18 - 35. How do the P/O ratios for NADH differ in ATP...Ch. 18 - 36. How many protons are required to synthesize...Ch. 18 - 37. During dietary restriction, amino acids may be...Ch. 18 - Prob. 38CQCh. 18 - 39. In coastal marine environments, high...Ch. 18 - Prob. 40CQCh. 18 - 41. (a) A simplistic interpretation of the Q cycle...Ch. 18 - Prob. 42CQCh. 18 - MORE TO EXPLORE Anaerobic organisms produce ATP by...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Biochemistry question. Please help with. Thanks in advance For each of the enzymes listed below, explain what the enzyme does including function, names (or structures) of the substrate and products and the pathway(s) (if applicable) it is/are found in. (a) ATP synthetase (b) succinate dehydrogenase (c) isocitrate lyase (d) acetyl CoA carboxylase (e) isocitrate dehydrogenase (f) malate dehydrogenasearrow_forwardDraw and name each alcohol and classify it as primary, secondary, or tertiary. Explain your answer thoroughly.arrow_forwardDraw the product of each reaction. If there are multiple products, draw only the major product. Explain your answer thoroughly.arrow_forward
- Identify the type of bond in the following disaccharides. Number your carbons to show work. Explain your answer thoroughly. Draw the number of carbons also.arrow_forwardDraw and explain your answer thoroughly: a. What is the molar mass of aspirin (C9H8O4)?b. What is the mass of 0.00225mol of aspirin?c. How many moles of aspirin are present in 500mg of aspirin?arrow_forwardGeranylgeranyl pyrophosphate 5 is converted by general acid-base catalysis to 6, and then to the natural product 7. For clarity only limited atom numbers are shown, but the main chain carbons are numbered 1 to 16, and the off-chain methyl substituents are numbered 17-20. A. Based on what you specified in A, use curly arrows on the drawing above to convert 5 to 6, and 6 to 7. Invoke general acids and general bases as needed, and draw in hydrogens as necessary . B. On the structure of 7, write in the atom numbers for the carbons marked with an asteriskarrow_forward
- α-Pinene (4) is synthesized enzymatically from nerol pyrophosphate 1. Drawn an arrow-pushing mechanism from 1 to 2 to 3 to 4; add explicit hydrogens to clarify, if needed.arrow_forwardA reverse phase column chromatography separates proteins according to their polarity. Which pentapeptide will be eluted FIRST when chromatographed at pH 7 using a reverse phase column such as a C-18 column? Peptide Sequence (from N-terminal to C-terminal) AKGED GAAVF ALLLI MCYAG GAAVF MCYAG ALLLI AKGEDarrow_forwardMelting of three DNA samples with varying lengths was monitored by increase of ultraviolet light absorbance at 260 nm. Which is the shortest DNA? A B Carrow_forward
- Select the CORRECT description of the peptide bond. The peptide bond can freely rotate around the peptide bond. The peptide bond is non-polar, hydrophobic and does not have a dipole. The peptide bond is most stable in the cis configuration. The peptide bond is rigid and planar. The peptide bond has a mix of single and double bond characters. The peptide bond is most stable in the trans configuration.arrow_forwardBelow is a fractional saturation curve for O2 binding to adult hemoglobin. Assume that curve Y represents a system at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve Z represents a system that ___________________ Curve Z: is at pH 7.4 with a higher than normal physiological level of 2,3-BPG. is at pH 7.4 with a normal physiological level of 2,3-BPG but with a decreased level of CO2. has a higher pH with a normal physiological level of 2,3-BPG. has a higher pH with a lower than physiological level of 2,3-BPG.arrow_forwardWhich is a homotropic positive effector of aspartate transcarbamoylase (ATCase)? oxygen CTP aspartate ATParrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Anaerobic Respiration; Author: Bozeman Science;https://www.youtube.com/watch?v=cDC29iBxb3w;License: Standard YouTube License, CC-BY