Entropy driven intermediates of oxygenation regulate hemoglobin allosteric behavior

E. Bucci, Zygmunt Gryczynski, A. Razynska, H. Kwansa

Research output: Contribution to journalArticle

Abstract

Temperature dependent oxygen binding capacity of human, bovine and fallow deer (Dama-Dama) Hb's, shows that at least one of the ligation intermediates absorbs heat, i.e. it is entropy driven [Bucci,E et.al Biochemistry 30:3195,1991;.Biochemistry 32:3519,1993; Bioph.J.in press; Johnson.et al.Biochemistry 31:10074; Biophys.Chem.59;107,1995). This phenomenon is also present in human Hb crosslinked between the beta82 Lys by dicarboxyl residues of increasing length, namely fumaryl (4 carbon), adipoyi (6 carbon) and sebacoyl (10 carbon) residues. The value of "n" and the overall oxygen affinity are correlated to the absorption of heat of the intermediate steps of ligation. Fumaryl-Hb has the lowest absorption of heat, the highest affinity and lowest cooperatively index. Adipoyl-Hb has the highest absorption of heat and the highest value of "n". It appears that positive enthalpy changes at the intermediates of oxygénation are a characteristic of the allosteric transitions of Hb. There is not enough information for assigning heat absorption to any of the interplays of the various conformations described for Hb and always available to the system besides the classic T and R, as R2 [Silva et al. JBC. 267:17248,1992] ], t [Liddington et al Nature 331: 725,1988], r [Wilson et al JMB 264:1996.1996], partially oxygenated Hb [Liddington et al. JMB 228:551,1992], partially ferric sebacoyl-Hb [Bucci et al Biochemistry 35:3418,1996], trimesyl-Hb [Shumacher et al Nature 375:84,1995] 4-carboxydnnamyl-Hb and 2,6-naphtalenedicarboxyl Hb, [Schumacher et al. PNAS 94:7841,1997]. Entropy driven steps may char acterize conformational changes still to be described.

Original languageEnglish
JournalFASEB Journal
Volume12
Issue number8
StatePublished - 1 Dec 1998

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Oxygenation
Entropy
entropy
Biochemistry
hemoglobin
Hemoglobins
Hot Temperature
biochemistry
heat
Cervus dama
Carbon
Ligation
carbon
Oxygen
oxygen
Deer
Trout
binding capacity
enthalpy
Conformations

Cite this

@article{8b07727b21214a72a24fc4f750e3c5df,
title = "Entropy driven intermediates of oxygenation regulate hemoglobin allosteric behavior",
abstract = "Temperature dependent oxygen binding capacity of human, bovine and fallow deer (Dama-Dama) Hb's, shows that at least one of the ligation intermediates absorbs heat, i.e. it is entropy driven [Bucci,E et.al Biochemistry 30:3195,1991;.Biochemistry 32:3519,1993; Bioph.J.in press; Johnson.et al.Biochemistry 31:10074; Biophys.Chem.59;107,1995). This phenomenon is also present in human Hb crosslinked between the beta82 Lys by dicarboxyl residues of increasing length, namely fumaryl (4 carbon), adipoyi (6 carbon) and sebacoyl (10 carbon) residues. The value of {"}n{"} and the overall oxygen affinity are correlated to the absorption of heat of the intermediate steps of ligation. Fumaryl-Hb has the lowest absorption of heat, the highest affinity and lowest cooperatively index. Adipoyl-Hb has the highest absorption of heat and the highest value of {"}n{"}. It appears that positive enthalpy changes at the intermediates of oxyg{\'e}nation are a characteristic of the allosteric transitions of Hb. There is not enough information for assigning heat absorption to any of the interplays of the various conformations described for Hb and always available to the system besides the classic T and R, as R2 [Silva et al. JBC. 267:17248,1992] ], t [Liddington et al Nature 331: 725,1988], r [Wilson et al JMB 264:1996.1996], partially oxygenated Hb [Liddington et al. JMB 228:551,1992], partially ferric sebacoyl-Hb [Bucci et al Biochemistry 35:3418,1996], trimesyl-Hb [Shumacher et al Nature 375:84,1995] 4-carboxydnnamyl-Hb and 2,6-naphtalenedicarboxyl Hb, [Schumacher et al. PNAS 94:7841,1997]. Entropy driven steps may char acterize conformational changes still to be described.",
author = "E. Bucci and Zygmunt Gryczynski and A. Razynska and H. Kwansa",
year = "1998",
month = "12",
day = "1",
language = "English",
volume = "12",
journal = "FASEB Journal",
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}

Entropy driven intermediates of oxygenation regulate hemoglobin allosteric behavior. / Bucci, E.; Gryczynski, Zygmunt; Razynska, A.; Kwansa, H.

In: FASEB Journal, Vol. 12, No. 8, 01.12.1998.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Entropy driven intermediates of oxygenation regulate hemoglobin allosteric behavior

AU - Bucci, E.

AU - Gryczynski, Zygmunt

AU - Razynska, A.

AU - Kwansa, H.

PY - 1998/12/1

Y1 - 1998/12/1

N2 - Temperature dependent oxygen binding capacity of human, bovine and fallow deer (Dama-Dama) Hb's, shows that at least one of the ligation intermediates absorbs heat, i.e. it is entropy driven [Bucci,E et.al Biochemistry 30:3195,1991;.Biochemistry 32:3519,1993; Bioph.J.in press; Johnson.et al.Biochemistry 31:10074; Biophys.Chem.59;107,1995). This phenomenon is also present in human Hb crosslinked between the beta82 Lys by dicarboxyl residues of increasing length, namely fumaryl (4 carbon), adipoyi (6 carbon) and sebacoyl (10 carbon) residues. The value of "n" and the overall oxygen affinity are correlated to the absorption of heat of the intermediate steps of ligation. Fumaryl-Hb has the lowest absorption of heat, the highest affinity and lowest cooperatively index. Adipoyl-Hb has the highest absorption of heat and the highest value of "n". It appears that positive enthalpy changes at the intermediates of oxygénation are a characteristic of the allosteric transitions of Hb. There is not enough information for assigning heat absorption to any of the interplays of the various conformations described for Hb and always available to the system besides the classic T and R, as R2 [Silva et al. JBC. 267:17248,1992] ], t [Liddington et al Nature 331: 725,1988], r [Wilson et al JMB 264:1996.1996], partially oxygenated Hb [Liddington et al. JMB 228:551,1992], partially ferric sebacoyl-Hb [Bucci et al Biochemistry 35:3418,1996], trimesyl-Hb [Shumacher et al Nature 375:84,1995] 4-carboxydnnamyl-Hb and 2,6-naphtalenedicarboxyl Hb, [Schumacher et al. PNAS 94:7841,1997]. Entropy driven steps may char acterize conformational changes still to be described.

AB - Temperature dependent oxygen binding capacity of human, bovine and fallow deer (Dama-Dama) Hb's, shows that at least one of the ligation intermediates absorbs heat, i.e. it is entropy driven [Bucci,E et.al Biochemistry 30:3195,1991;.Biochemistry 32:3519,1993; Bioph.J.in press; Johnson.et al.Biochemistry 31:10074; Biophys.Chem.59;107,1995). This phenomenon is also present in human Hb crosslinked between the beta82 Lys by dicarboxyl residues of increasing length, namely fumaryl (4 carbon), adipoyi (6 carbon) and sebacoyl (10 carbon) residues. The value of "n" and the overall oxygen affinity are correlated to the absorption of heat of the intermediate steps of ligation. Fumaryl-Hb has the lowest absorption of heat, the highest affinity and lowest cooperatively index. Adipoyl-Hb has the highest absorption of heat and the highest value of "n". It appears that positive enthalpy changes at the intermediates of oxygénation are a characteristic of the allosteric transitions of Hb. There is not enough information for assigning heat absorption to any of the interplays of the various conformations described for Hb and always available to the system besides the classic T and R, as R2 [Silva et al. JBC. 267:17248,1992] ], t [Liddington et al Nature 331: 725,1988], r [Wilson et al JMB 264:1996.1996], partially oxygenated Hb [Liddington et al. JMB 228:551,1992], partially ferric sebacoyl-Hb [Bucci et al Biochemistry 35:3418,1996], trimesyl-Hb [Shumacher et al Nature 375:84,1995] 4-carboxydnnamyl-Hb and 2,6-naphtalenedicarboxyl Hb, [Schumacher et al. PNAS 94:7841,1997]. Entropy driven steps may char acterize conformational changes still to be described.

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