BIOCHEMISTRY
8th Edition
ISBN: 9781319296186
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 20, Problem 8P
Interpretation Introduction
Interpretation:
The reason for the decrease in activity of Rubisco in an atmosphere devoid of CO2 but rich in O2, should be determined.
Concept introduction:
Ribulose 1, 5-bisphosphate carboxylase/ oxygenase is a key enzyme in Calvin cycle as well as photosynthesis. During the process of carbon fixation, rubisco converts inorganic carbon dioxide into an organic molecule in the first stage of the Calvin cycle.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Biochemistry
Assuming 2.5 molecules of ATP per oxidation of NADH/(H+) and 1.5molecules of ATP per oxidation of FADH2, how many ATP are produced per molecule of pyruvate?
Please help. Thank you
1. How would you explain the term ‘good food’?
2. How would you define Nutrition?
3. Nutrients are generally categorised into two forms. Discuss.
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.
Chapter 20 Solutions
BIOCHEMISTRY
Ch. 20 - Prob. 1PCh. 20 - Prob. 2PCh. 20 - Prob. 3PCh. 20 - Prob. 4PCh. 20 - Prob. 5PCh. 20 - Prob. 6PCh. 20 - Prob. 7PCh. 20 - Prob. 8PCh. 20 - Prob. 9PCh. 20 - Prob. 10P
Ch. 20 - Prob. 11PCh. 20 - Prob. 12PCh. 20 - Prob. 13PCh. 20 - Prob. 14PCh. 20 - Prob. 15PCh. 20 - Prob. 16PCh. 20 - Prob. 17PCh. 20 - Prob. 18PCh. 20 - Prob. 19PCh. 20 - Prob. 20PCh. 20 - Prob. 21PCh. 20 - Prob. 22PCh. 20 - Prob. 23PCh. 20 - Prob. 24PCh. 20 - Prob. 25PCh. 20 - Prob. 26PCh. 20 - Prob. 27PCh. 20 - Prob. 28PCh. 20 - Prob. 29PCh. 20 - Prob. 30PCh. 20 - Prob. 31PCh. 20 - Prob. 32PCh. 20 - Prob. 33PCh. 20 - Prob. 34PCh. 20 - Prob. 35PCh. 20 - Prob. 36PCh. 20 - Prob. 37PCh. 20 - Prob. 38PCh. 20 - Prob. 39P
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.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!arrow_forwardBiochemistry 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?arrow_forwardBiochemistry 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_forward
- Draw 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_forwardIdentify 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_forward
- Draw 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_forwardα-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_forward
- A 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_forwardSelect 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_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