In class, we discussed how H146 of the LaTeX: / betaβ-chain of normal adult hemoglobin ends up in close proximity to D94 on the same chain when oxygen is delivered to the tissues. In hemoglobin Hiroshima, however, H146 on the LaTeX: / betaβ-chain has been changed to a D through mutation. a) What effect, if any, does this mutation have on oxygen binding by hemoglobin Hiroshima, compared to normal hemoglobin? Explain in detail.

Question

Baby Boo

Biology

8 April, 02:23

In class, we discussed how H146 of the LaTeX: / betaβ-chain of normal adult hemoglobin ends up in close proximity to D94 on the same chain when oxygen is delivered to the tissues. In hemoglobin Hiroshima, however, H146 on the LaTeX: / betaβ-chain has been changed to a D through mutation. a) What effect, if any, does this mutation have on oxygen binding by hemoglobin Hiroshima, compared to normal hemoglobin? Explain in detail.

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Answers (1)

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Lyric Cross · Answer 1

Hemoglobin Hiroshima is a variant known to reduce the oxygen affinity and to increase the pH.

Explanation:

Hemoglobin Hiroshima is produced by a mutation in the β chain of the hemoglobin protein (histidine >> aspartate at position 146). This mutation is known to affect the kinetic properties of the hemoglobin protein, thereby having functional consequences that may lead to mild erythremia, a pathology characterized by an increase of red blood cells.