DOI: 10.1002/prot.340020109. Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin

Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin

10.1002/prot.340020109

Crossref journal-article

Wiley

Proteins: Structure, Function, and Bioinformatics (311)

Abstract

AbstractA few years ago we reported that histidine (HC3) 146β plays a major role in the pH‐dependent propeties of the R‐state of human hemoglobin, accounting for close to 50% of the R‐state Bohr effect. We have extended these studies by examining the role of arginine 141α, another group known to affect the overall Bohr effect. We have compared the pH dependencies of the rate constants for the dissociation and combination of the fourth carbon monoxide molecule, I4 and I′4, respectively, for native hemoglobin A (HbA) and a control reconstututed HbA, and des‐(Arg 141α) HbA, the hemoglobin molecule resulting from the enzymatic removal of the C–terminal arginine of the α‐chain of human Hb. From these kinetic contants the pH dependence of L4, by about 80% between pH 6 and 8, where the aldkaline Bohr effect normally occurs, The sum of the effects of the removal of His 146β and of Arg 141α is grater than 100%. This suggests that at least one of these modifications altrs the contrubutions of other residues of this Bohr effect.

Bibliography

Kwiatkowski, L. D., & Noble, R. W. (1987). Contribution of arginine (HC3) 141Î± to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin. Proteins: Structure, Function, and Bioinformatics, 2(1), 72â77. Portico.

Authors 2

Laura D. Kwiatkowski (first)
Robert W. Noble (additional)

References 36 Referenced 3

10.1016/S0022-2836(65)80285-6
10.1016/S0021-9258(19)41706-7 / J. Biol. Chem. / pH dependence of the Adair constants of human hemoglobin by Imai K. (1975)
10.1016/S0021-9258(17)33000-4 / J. Biol. Chem. / Kinetic studies on the binding affinity of human hemoglobin for the 4th carbon monoxide molecule, L4 by De Young A. (1976)
10.1038/228766a0
10.1016/0022-2836(74)90244-7
10.1016/0022-2836(75)90128-X
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{'key': 'e_1_2_1_9_2', 'first-page': '1240', 'volume': '222', 'author': 'Perutz M.F.', 'year': '1969', 'journal-title': 'Identification of residues responsible for the alkaline Bohr effect in hemoglobin.'} / Identification of residues responsible for the alkaline Bohr effect in hemoglobin. by Perutz M.F. (1969)
10.1016/S0021-9258(19)41315-X / J. Biol. Chem. / Determination of the pK values for the α‐amino groups of human hemoglobin by Garner M.H. (1975)
10.1016/S0021-9258(17)40546-1 / J. Biol. Chem. / Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3‐diphosphoglycerate by Matthew J.B. (1977)
10.1073/pnas.70.4.1246
10.1021/bi00546a033
10.1021/bi00263a029
10.1111/j.1432-1033.1978.tb12749.x
10.1016/S0021-9258(18)34214-5 / J. Biol. Chem. / The contribution of histidine (HC3) (146α) to the R state Bohr effect of human hemoglobin by Kwiatkowski L.D. (1982)
{'key': 'e_1_2_1_17_2', 'first-page': '651', 'article-title': 'The effect of removal of arginine 141α on a pH dependent kinetic property of the R state of human hemoglobin A', 'volume': '41', 'author': 'Kwiatkowski L.D.', 'year': '1982', 'journal-title': 'Fed. Proc.'} / Fed. Proc. / The effect of removal of arginine 141α on a pH dependent kinetic property of the R state of human hemoglobin A by Kwiatkowski L.D. (1982)
10.1016/S0021-9258(18)93675-6 / J. Biol. Chem. / Preparation and properties of α‐ and β‐chains from human hemoglobin by Geraci G. (1969)
10.1016/S0021-9258(19)43357-7 / J. Biol. Chem. / Role of the α amino groups of the α and β‐ chains of human hemoglobin in oxygen‐linked binding of carbon dioxide by Kilmartin J.V. (1973)
10.1021/ja01646a025
10.1016/0076-6879(81)76111-1
10.1042/bj0910161
10.1016/B978-0-12-151301-6.50009-5
10.1016/0022-2836(73)90041-7
10.1016/S0021-9258(19)86450-5 / J. Biol. Chem. / X‐ray diffraction and solution studies on specificially carbamylated human hemoglobin A by O'Donnell S. (1979)
10.1016/S0022-2836(83)80313-1
10.1101/SQB.1972.036.01.040
10.1016/0014-5793(76)80663-1
{'key': 'e_1_2_1_29_2', 'first-page': '9465', 'article-title': 'Structural and functional studies of hemoglobin Suresnes (Arg 141α2→His β2)', 'volume': '255', 'author': 'Poyart C.', 'year': '1980', 'journal-title': 'J. Biol. Chem.'} / J. Biol. Chem. / Structural and functional studies of hemoglobin Suresnes (Arg 141α2→His β2) by Poyart C. (1980)
10.1093/oxfordjournals.jbchem.a133091 / J. Biochem. / Hemoglobin Legnano (α2141(HC3) Arg→Leu β2). A new high oxygen affinity variant by Giuliani A. (1980)
10.1172/JCI111749
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10.1016/0022-2836(85)90016-6
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10.1073/pnas.82.16.5347

Dates

Type	When
Created	20 years, 3 months ago (May 28, 2005, 8:57 p.m.)
Deposited	1 year, 10 months ago (Oct. 20, 2023, 10:28 a.m.)
Indexed	1 year, 10 months ago (Oct. 31, 2023, 2:19 a.m.)
Issued	38 years, 8 months ago (Jan. 1, 1987)
Published	38 years, 8 months ago (Jan. 1, 1987)
Published Online	21 years, 7 months ago (Feb. 3, 2004)
Published Print	38 years, 8 months ago (Jan. 1, 1987)

Funders 0

None

BibTeX

@article{Kwiatkowski_1987, title={Contribution of arginine (HC3) 141α to the Bohr effect of the fourth binding step in the reaction of ligand with human hemoglobin}, volume={2}, ISSN={1097-0134}, url={http://dx.doi.org/10.1002/prot.340020109}, DOI={10.1002/prot.340020109}, number={1}, journal={Proteins: Structure, Function, and Bioinformatics}, publisher={Wiley}, author={Kwiatkowski, Laura D. and Noble, Robert W.}, year={1987}, month=jan, pages={72–77} }

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