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F helix F hellx HN- O2 HN- O2 (a) The effect of O, binding according to the Perutz model: The F helix is drawn toward the heme. F helix F helx HN- O2 HN- (b) Now lacking a covalent connection to the heme, the F helix is not disturbed by O, binding, and there is significantly reduced cooperativity. A FIGURE 7.26 The effect of replacing the proximal histidine in hemoglobin with a glycine residue and adding a noncovalently bonded imidazole.

F helix F hellx HN- O2 HN- O2 (a) The effect of O, binding according to the Perutz model: The F helix is drawn toward the heme. F helix F helx HN- O2 HN- (b) Now lacking a covalent connection to the heme, the F helix is not disturbed by O, binding, and there is significantly reduced cooperativity. A FIGURE 7.26 The effect of replacing the proximal histidine in hemoglobin with a glycine residue and adding a noncovalently bonded imidazole.

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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In the experiments of Barrick et al. (as shown), it was observed that
replacement of histidine by a noncovalently bonded imidazole not only
reduced cooperativity but also increased the oxygen affinity of the hemoglobin. Suggest an explanation.

F helix F hellx HN- O2 HN- O2 (a) The effect of O, binding according to the Perutz model: The F helix is drawn toward the heme. F helix F helx HN- O2 HN- (b) Now lacking a covalent connection to the heme, the F helix is not disturbed by O, binding, and there is significantly reduced cooperativity. A FIGURE 7.26 The effect of replacing the proximal histidine in hemoglobin with a glycine residue and adding a noncovalently bonded imidazole.
Transcribed Image Text:F helix F hellx HN- O2 HN- O2 (a) The effect of O, binding according to the Perutz model: The F helix is drawn toward the heme. F helix F helx HN- O2 HN- (b) Now lacking a covalent connection to the heme, the F helix is not disturbed by O, binding, and there is significantly reduced cooperativity. A FIGURE 7.26 The effect of replacing the proximal histidine in hemoglobin with a glycine residue and adding a noncovalently bonded imidazole.
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