Oxygen binding to α-subunits in high-salt crystals of T-state hemoglobin

Gregory B. Vásquez; Xinhua Ji; Igor Pechik; Clara Fronticelli; Gary L. Gilliland

doi:10.2174/092986650602221108150658

Oxygen binding to α-subunits in high-salt crystals of T-state hemoglobin

Gregory B. Vásquez
, Xinhua Ji
, Igor Pechik
, Clara Fronticelli
, Gary L. Gilliland

Research output: Contribution to journal › Article › peer-review

Abstract

The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 Å and 1.8 Å resolution, respectively. Oxygen molecules fully occupy the α₁-heme and partially occupy the α₂-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.

Original language	English (US)
Pages (from-to)	59-66
Number of pages	8
Journal	Protein and Peptide Letters
Volume	6
Issue number	2
DOIs	https://doi.org/10.2174/092986650602221108150658
State	Published - 1999
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Biochemistry

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title = "Oxygen binding to α-subunits in high-salt crystals of T-state hemoglobin",

abstract = "The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 {\AA} and 1.8 {\AA} resolution, respectively. Oxygen molecules fully occupy the α1-heme and partially occupy the α2-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.",

author = "V{\'a}squez, \{Gregory B.\} and Xinhua Ji and Igor Pechik and Clara Fronticelli and Gilliland, \{Gary L.\}",

year = "1999",

doi = "10.2174/092986650602221108150658",

language = "English (US)",

volume = "6",

pages = "59--66",

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T1 - Oxygen binding to α-subunits in high-salt crystals of T-state hemoglobin

AU - Vásquez, Gregory B.

AU - Ji, Xinhua

AU - Pechik, Igor

AU - Fronticelli, Clara

AU - Gilliland, Gary L.

PY - 1999

Y1 - 1999

N2 - The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 Å and 1.8 Å resolution, respectively. Oxygen molecules fully occupy the α1-heme and partially occupy the α2-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.

AB - The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 Å and 1.8 Å resolution, respectively. Oxygen molecules fully occupy the α1-heme and partially occupy the α2-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.

UR - https://www.scopus.com/pages/publications/0346491823

UR - https://www.scopus.com/pages/publications/0346491823#tab=citedBy

U2 - 10.2174/092986650602221108150658

DO - 10.2174/092986650602221108150658

M3 - Article

AN - SCOPUS:0346491823

SN - 0929-8665

VL - 6

SP - 59

EP - 66

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 2

ER -

Oxygen binding to α-subunits in high-salt crystals of T-state hemoglobin

Abstract

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