BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 24, Problem 8P
Interpretation Introduction
Interpretation:
Whether the statement is true or false should be determined.
Concept introduction:
Nitrogen fixation is the process by which the molecular nitrogen of the atmosphere is converted into ammonia or other nitrogenous compounds. Atmospheric nitrogen is unreactive and
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Select all that apply.
What is true about the conformational aspects of coupling?
O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change.
O The conformational states interconvert as a result of proton flux through the synthase.
There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T).
Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis.
The Fo portion of ATP synthase acts as a rotary motor.
For 100 words. What are the two essential requirements to effectively carry out metabolic work?
Hi, help please. Discuss each method of regulating phosphofructokinase below as indicated by the circle. Discuss 1.) The type of regulation occurring, 2.) What compound or condition performs the regulation, 3.) How/why it influences the enzyme activity.
Chapter 24 Solutions
BIOCHEMISTRY
Ch. 24 - Prob. 1PCh. 24 - Prob. 2PCh. 24 - Prob. 3PCh. 24 - Prob. 4PCh. 24 - Prob. 5PCh. 24 - Prob. 6PCh. 24 - Prob. 7PCh. 24 - Prob. 8PCh. 24 - Prob. 9PCh. 24 - Prob. 10P
Ch. 24 - Prob. 11PCh. 24 - Prob. 12PCh. 24 - Prob. 13PCh. 24 - Prob. 14PCh. 24 - Prob. 15PCh. 24 - Prob. 16PCh. 24 - Prob. 17PCh. 24 - Prob. 18PCh. 24 - Prob. 19PCh. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - Prob. 25PCh. 24 - Prob. 26PCh. 24 - Prob. 27PCh. 24 - Prob. 28PCh. 24 - Prob. 29PCh. 24 - Prob. 30PCh. 24 - Prob. 31PCh. 24 - Prob. 32PCh. 24 - Prob. 33PCh. 24 - Prob. 34PCh. 24 - Prob. 35PCh. 24 - Prob. 36PCh. 24 - Prob. 37PCh. 24 - Prob. 38PCh. 24 - Prob. 39PCh. 24 - Prob. 40P
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
- Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?arrow_forwardHelp please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!arrow_forwardRequired partner. Aminotransferases require which of the following cofactors: a. NAD+/NADP+NAD+/NADP+ b. Pyridoxal phosphate c. Thiamine pyrophosphate d. Biopterinarrow_forward
- What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1arrow_forwardIn full details. Explain the significance of redox potentials formed by redox pairs in the electron transport chain.arrow_forward. Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reactionarrow_forward
- Draw Gluconeogenesis. Please make sure to state all the enzymes and co-factors for each step of the pathway.arrow_forwardQuestion #1: Choanoflagelletes are a unicellular ancestor to animals. One observation to support this hypothesis is the appearance of adhesion molecules that are key to the development of multiceullarity. Bulk transport Gap junctions Animals. Adhesion, cell signaling Single-celled :} Insects, mammals, and other animals with bilateral symmetry (~10,000,000) Jellyfish and their relatives (10,000) } Sponges (10,000) Choanoflagellates (150) Despite their simple unicellular lifestyle they express adhesion molecules including cadherins and lectins (King et al., 2003) but don't seem to have molecules that are typically found in the extracellular matrix such as integrins or laminins (Williams et al., 2014). Design a microscopy experiment to test the assertion that choanoflagellates have (some) adhesion molecules and those molecules play a similar role in a closely related animal like sponges.arrow_forwardI. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4arrow_forward
- Draw Glycolysis. Please make sure to state all the enzymes and co-factors for each step of the pathway.arrow_forwardMany enzyme -catalyzed reactions are consistent with a modified version of the Michaelis -Menten mechanism in which the second step is also reversible. For this mechanism obtain an expression for the rate of formation of product and find its limiting behavior for large and small concentrations of substrate using steady state approximationarrow_forwardA7. Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.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. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals 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 LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals 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