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Vhich one of the following choices contains ONLY TRUE statements? O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(l) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem group. The propionate substituents on the porphyrin ring are used to form amide bonds with lysine residues on the protein. In deoxymyoglobin the haem group contains Fe(ll) in the low spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(l) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O Myoglobin is an oxygen binding protein that stores oxygen in the muscles. Myoglobin contains a Cu/Zn active site. The copper(II) is in a square pyramidal environment whereas the zinc(II) site is in a tetrahedral environment. O Myoglobin is an enzyme that both reduced and oxidises superoxide.

Vhich one of the following choices contains ONLY TRUE statements? O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(l) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem group. The propionate substituents on the porphyrin ring are used to form amide bonds with lysine residues on the protein. In deoxymyoglobin the haem group contains Fe(ll) in the low spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(l) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O Myoglobin is an oxygen binding protein that stores oxygen in the muscles. Myoglobin contains a Cu/Zn active site. The copper(II) is in a square pyramidal environment whereas the zinc(II) site is in a tetrahedral environment. O Myoglobin is an enzyme that both reduced and oxidises superoxide.

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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Which one of the following choices contains ONLY TRUE statements? O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(l) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem group. The propionate substituents on the porphyrin ring are used to form amide bonds with lysine residues on the protein. In deoxymyoglobin the haem group contains Fe(ll) in the low spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(ll) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O Myoglobin is an oxygen binding protein that stores oxygen in the muscles. Myoglobin contains a Cu/Zn active site. The copper(II) is in a square pyramidal environment whereas the zinc(lI) site is in a tetrahedral environment. O Myoglobin is an enzyme that both reduced and oxidises superoxide.
Transcribed Image Text:Which one of the following choices contains ONLY TRUE statements? O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(l) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem group. The propionate substituents on the porphyrin ring are used to form amide bonds with lysine residues on the protein. In deoxymyoglobin the haem group contains Fe(ll) in the low spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O The active site of myoglobin contains a haem prosthetic group. The propionate substituents on the porphyrin ring are involved in hydrogen-bonding interactions with water molecules. In deoxymyoglobin the haem group contains Fe(ll) in the high spin state. Upon binding dioxygen the iron undergoes a change in spin state that reduces its ionic radii inducing a structural change in the protein. O Myoglobin is an oxygen binding protein that stores oxygen in the muscles. Myoglobin contains a Cu/Zn active site. The copper(II) is in a square pyramidal environment whereas the zinc(lI) site is in a tetrahedral environment. O Myoglobin is an enzyme that both reduced and oxidises superoxide.
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