The water effect on allosteric regulation of hemoglobin probed in water glucose and water glycine solutions

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.creatorColombo, Marcio Francisco [UNESP]
dc.creatorBonilla-Rodriguez, Gustave O. [UNESP]
dc.date2014-05-27T11:18:04Z
dc.date2014-05-27T11:18:04Z
dc.date1996-03-01
dc.date.accessioned2023-09-12T07:50:36Z
dc.date.available2023-09-12T07:50:36Z
dc.identifierhttp://dx.doi.org/10.1074/jbc.271.9.4895
dc.identifierJournal of Biological Chemistry, v. 271, n. 9, p. 4895-4899, 1996.
dc.identifier0021-9258
dc.identifierhttp://hdl.handle.net/11449/132347
dc.identifier10.1074/jbc.271.9.4895
dc.identifierWOS:A1996TX69700051
dc.identifier2-s2.0-0029867430
dc.identifier3425817209646054
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8781626
dc.descriptionWe have previously proposed a role of hydration in the allosteric control of hemoglobin based on the effect of varying concentrations of polyols and polyethers on the human hemoglobin oxygen affinity and on the solution water activity (Colombo, M. F., Rau, D. C., and Parsegian, V. A. (1992) Science 256, 655-659). Here, the original analyses are extended to test the possibility of concomitant solute and water allosteric binding and by introducing the bulk dielectric constant as a variable in our experiments. We present data which indicate that glycine and glucose influence HbA oxygen affinity to the same extent, despite the fact that glycine increases and glucose decreases the bulk dielectric constant of the solution. Furthermore, we derive an equation linking changes in oxygen affinity to changes in differential solute and water binding to test critically the possibility of neutral solute heterotropic binding. Applied to the data, these analyses support our original interpretation that neutral solutes act indirectly on the regulation of allosteric behavior of hemoglobin by varying the chemical potential of water in solution. This leads to a displacement of the equilibrium between Hb conformational states in proportion to their differential hydration.
dc.descriptionDepartamento de Física Inst. Biociencias, Letras Cie. E. Univ. Estadual Paulista Julio M., São Paulo State, CEP 15054-000
dc.descriptionDepto. de Física IBILCE-UNESP, Rua Cristovão Colombo 2265, S. Jose Rio Preto S.P. CEP 15054-000
dc.descriptionDepto. de Física IBILCE-UNESP, Rua Cristovão Colombo 2265, S. Jose Rio Preto S.P. CEP 15054-000
dc.format4895-4899
dc.languageeng
dc.publisherAmer Soc Biochemistry Molecular Biology Inc
dc.relationJournal of Biological Chemistry
dc.relation4.010
dc.relation2,672
dc.rightsAcesso restrito
dc.sourceScopus
dc.subjectglycine
dc.subjecthemoglobin
dc.subjectallosterism
dc.subjectbinding site
dc.subjectcross linking
dc.subjectdielectric constant
dc.subjectglucose metabolism
dc.subjecthuman
dc.subjecthuman cell
dc.subjecthydration
dc.subjecthydrophilicity
dc.subjectoxygen affinity
dc.subjectphotolysis
dc.subjectpriority journal
dc.subjectprotein conformation
dc.subjectwater metabolism
dc.subjectAdult
dc.subjectAllosteric Regulation
dc.subjectChlorides
dc.subjectElectrochemistry
dc.subjectGlucose
dc.subjectGlycine
dc.subjectHemoglobins
dc.subjectHumans
dc.subjectKinetics
dc.subjectMathematics
dc.subjectModels, Theoretical
dc.subjectOxyhemoglobins
dc.subjectSolutions
dc.subjectWater
dc.titleThe water effect on allosteric regulation of hemoglobin probed in water glucose and water glycine solutions
dc.typeArtigo


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