Characteristic of aromatic amino acid substitution at α96 of hemoglobin

Jong Whan Choi, Jong Ho Lee, Ho Lee Kwang, Hyean Woo Lee, Hyung Sohn Joon, Ho Yoon Joon, Byung Il Yeh, Kyu Park Seung, Jae Lee Kyu, Hyun Won Kim

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Replacement of valine by tryptophan or tyrosine at position α96 of the α chain (α96Val), located in the α1β 2 subunit interface of hemoglobin leads to low oxygen affinity hemoglobin, and has been suggested to be due to the extra stability introduced by an aromatic amino acid at the α96 position. The characteristic of aromatic amino acid substitution at the α96 of hemoglobin has been further investigated by producing double mutant r Hb (α42Tyr → Phe, α96Val → Trp). r Hb (α42Tyr → Phe) is known to exhibit almost no cooperativity in binding oxygen, and possesses high oxygen affinity due to the disruption of the hydrogen bond between α42Tyr and β99Asp in the α1β2 subunit interface of deoxy Hb A. The second mutation, α96Val → Trp, may compensate the functional defects of r Hb (α42Tyr → Phe), if the stability due to the introduction of trypophan at the α96 position is strong enough to overcome the defect of r Hb (α42Tyr → Phe). Double mutant r Hb (α42Tyr → Phe, α96Val → Trp) exhibited almost no cooperativity in binding oxygen and possessed high oxygen affinity, similarly to that of r Hb (α42Tyr → Phe). 1H NMR spectroscopic data of r Hb (α42Tyr → Phe, α96Val → Trp) also showed a very unstable deoxy-quaternary structure. The present investigation has demonstrated that the presence of the crucible hydrogen bond between α42Tyr and β99Asp is essential for the novel oxygen binding properties of deoxy Hb (α96Val → Trp).

Original languageEnglish
Pages (from-to)115-119
Number of pages5
JournalJournal of Biochemistry and Molecular Biology
Volume38
Issue number1
Publication statusPublished - 2005 Dec 1

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Aromatic Amino Acids
Amino Acid Substitution
Hemoglobins
Substitution reactions
Oxygen
Hydrogen
Hydrogen bonds
Hemoglobin Subunits
Defects
Crucibles
Valine
Tryptophan
Tyrosine
Nuclear magnetic resonance
Mutation

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Choi, J. W., Lee, J. H., Kwang, H. L., Lee, H. W., Joon, H. S., Joon, H. Y., ... Kim, H. W. (2005). Characteristic of aromatic amino acid substitution at α96 of hemoglobin. Journal of Biochemistry and Molecular Biology, 38(1), 115-119.
Choi, Jong Whan ; Lee, Jong Ho ; Kwang, Ho Lee ; Lee, Hyean Woo ; Joon, Hyung Sohn ; Joon, Ho Yoon ; Yeh, Byung Il ; Seung, Kyu Park ; Kyu, Jae Lee ; Kim, Hyun Won. / Characteristic of aromatic amino acid substitution at α96 of hemoglobin. In: Journal of Biochemistry and Molecular Biology. 2005 ; Vol. 38, No. 1. pp. 115-119.
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title = "Characteristic of aromatic amino acid substitution at α96 of hemoglobin",
abstract = "Replacement of valine by tryptophan or tyrosine at position α96 of the α chain (α96Val), located in the α1β 2 subunit interface of hemoglobin leads to low oxygen affinity hemoglobin, and has been suggested to be due to the extra stability introduced by an aromatic amino acid at the α96 position. The characteristic of aromatic amino acid substitution at the α96 of hemoglobin has been further investigated by producing double mutant r Hb (α42Tyr → Phe, α96Val → Trp). r Hb (α42Tyr → Phe) is known to exhibit almost no cooperativity in binding oxygen, and possesses high oxygen affinity due to the disruption of the hydrogen bond between α42Tyr and β99Asp in the α1β2 subunit interface of deoxy Hb A. The second mutation, α96Val → Trp, may compensate the functional defects of r Hb (α42Tyr → Phe), if the stability due to the introduction of trypophan at the α96 position is strong enough to overcome the defect of r Hb (α42Tyr → Phe). Double mutant r Hb (α42Tyr → Phe, α96Val → Trp) exhibited almost no cooperativity in binding oxygen and possessed high oxygen affinity, similarly to that of r Hb (α42Tyr → Phe). 1H NMR spectroscopic data of r Hb (α42Tyr → Phe, α96Val → Trp) also showed a very unstable deoxy-quaternary structure. The present investigation has demonstrated that the presence of the crucible hydrogen bond between α42Tyr and β99Asp is essential for the novel oxygen binding properties of deoxy Hb (α96Val → Trp).",
author = "Choi, {Jong Whan} and Lee, {Jong Ho} and Kwang, {Ho Lee} and Lee, {Hyean Woo} and Joon, {Hyung Sohn} and Joon, {Ho Yoon} and Yeh, {Byung Il} and Seung, {Kyu Park} and Kyu, {Jae Lee} and Kim, {Hyun Won}",
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Choi, JW, Lee, JH, Kwang, HL, Lee, HW, Joon, HS, Joon, HY, Yeh, BI, Seung, KP, Kyu, JL & Kim, HW 2005, 'Characteristic of aromatic amino acid substitution at α96 of hemoglobin', Journal of Biochemistry and Molecular Biology, vol. 38, no. 1, pp. 115-119.

Characteristic of aromatic amino acid substitution at α96 of hemoglobin. / Choi, Jong Whan; Lee, Jong Ho; Kwang, Ho Lee; Lee, Hyean Woo; Joon, Hyung Sohn; Joon, Ho Yoon; Yeh, Byung Il; Seung, Kyu Park; Kyu, Jae Lee; Kim, Hyun Won.

In: Journal of Biochemistry and Molecular Biology, Vol. 38, No. 1, 01.12.2005, p. 115-119.

Research output: Contribution to journalArticle

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T1 - Characteristic of aromatic amino acid substitution at α96 of hemoglobin

AU - Choi, Jong Whan

AU - Lee, Jong Ho

AU - Kwang, Ho Lee

AU - Lee, Hyean Woo

AU - Joon, Hyung Sohn

AU - Joon, Ho Yoon

AU - Yeh, Byung Il

AU - Seung, Kyu Park

AU - Kyu, Jae Lee

AU - Kim, Hyun Won

PY - 2005/12/1

Y1 - 2005/12/1

N2 - Replacement of valine by tryptophan or tyrosine at position α96 of the α chain (α96Val), located in the α1β 2 subunit interface of hemoglobin leads to low oxygen affinity hemoglobin, and has been suggested to be due to the extra stability introduced by an aromatic amino acid at the α96 position. The characteristic of aromatic amino acid substitution at the α96 of hemoglobin has been further investigated by producing double mutant r Hb (α42Tyr → Phe, α96Val → Trp). r Hb (α42Tyr → Phe) is known to exhibit almost no cooperativity in binding oxygen, and possesses high oxygen affinity due to the disruption of the hydrogen bond between α42Tyr and β99Asp in the α1β2 subunit interface of deoxy Hb A. The second mutation, α96Val → Trp, may compensate the functional defects of r Hb (α42Tyr → Phe), if the stability due to the introduction of trypophan at the α96 position is strong enough to overcome the defect of r Hb (α42Tyr → Phe). Double mutant r Hb (α42Tyr → Phe, α96Val → Trp) exhibited almost no cooperativity in binding oxygen and possessed high oxygen affinity, similarly to that of r Hb (α42Tyr → Phe). 1H NMR spectroscopic data of r Hb (α42Tyr → Phe, α96Val → Trp) also showed a very unstable deoxy-quaternary structure. The present investigation has demonstrated that the presence of the crucible hydrogen bond between α42Tyr and β99Asp is essential for the novel oxygen binding properties of deoxy Hb (α96Val → Trp).

AB - Replacement of valine by tryptophan or tyrosine at position α96 of the α chain (α96Val), located in the α1β 2 subunit interface of hemoglobin leads to low oxygen affinity hemoglobin, and has been suggested to be due to the extra stability introduced by an aromatic amino acid at the α96 position. The characteristic of aromatic amino acid substitution at the α96 of hemoglobin has been further investigated by producing double mutant r Hb (α42Tyr → Phe, α96Val → Trp). r Hb (α42Tyr → Phe) is known to exhibit almost no cooperativity in binding oxygen, and possesses high oxygen affinity due to the disruption of the hydrogen bond between α42Tyr and β99Asp in the α1β2 subunit interface of deoxy Hb A. The second mutation, α96Val → Trp, may compensate the functional defects of r Hb (α42Tyr → Phe), if the stability due to the introduction of trypophan at the α96 position is strong enough to overcome the defect of r Hb (α42Tyr → Phe). Double mutant r Hb (α42Tyr → Phe, α96Val → Trp) exhibited almost no cooperativity in binding oxygen and possessed high oxygen affinity, similarly to that of r Hb (α42Tyr → Phe). 1H NMR spectroscopic data of r Hb (α42Tyr → Phe, α96Val → Trp) also showed a very unstable deoxy-quaternary structure. The present investigation has demonstrated that the presence of the crucible hydrogen bond between α42Tyr and β99Asp is essential for the novel oxygen binding properties of deoxy Hb (α96Val → Trp).

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