Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein

Bruno Giardina; Paolo Ascenzi; Maria Elisabetta Clementi; Giampiero De Sanctis; Menico Rizzi; Massimo Coletta

doi:10.1074/jbc.271.29.16999

Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein

Bruno Giardina
, Paolo Ascenzi
, Maria Elisabetta Clementi
, Giampiero De Sanctis
, Menico Rizzi
, Massimo Coletta

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

Abstract

The effect of lactate on O₂ binding properties of sperm whale and horse heart myoglobins (Mb) has been investigated at moderately acid pH (i.e. pH 6.5, a condition which may be achieved in vivo under a physical effort). Addition of lactate brings about a decrease of O₂ affinity (i.e. an increase of P₅₀) in sperm whale and horse heart myoglobins. Accordingly, lactate shows a different affinity for the deoxygenated and oxygenated form, behaving as a heterotropic modulator. The lactate effect on O₂ affinity appears to differ for sperm whale and horse heart Mb, δlogP₅₀ being ≃1.0 and ≃0.4, respectively. From the kinetic viewpoint, the variation of O₂ affinity for both myoglobins can be attributed mainly to a decrease of the kinetic association rate constant for ligand binding.

Original language	English
Pages (from-to)	16999-17001
Number of pages	3
Journal	Journal of Biological Chemistry
Volume	271
Issue number	29
DOIs	https://doi.org/10.1074/jbc.271.29.16999
Publication status	Published - 1996
Externally published	Yes

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title = "Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein",

abstract = "The effect of lactate on O2 binding properties of sperm whale and horse heart myoglobins (Mb) has been investigated at moderately acid pH (i.e. pH 6.5, a condition which may be achieved in vivo under a physical effort). Addition of lactate brings about a decrease of O2 affinity (i.e. an increase of P50) in sperm whale and horse heart myoglobins. Accordingly, lactate shows a different affinity for the deoxygenated and oxygenated form, behaving as a heterotropic modulator. The lactate effect on O2 affinity appears to differ for sperm whale and horse heart Mb, δlogP50 being ≃1.0 and ≃0.4, respectively. From the kinetic viewpoint, the variation of O2 affinity for both myoglobins can be attributed mainly to a decrease of the kinetic association rate constant for ligand binding.",

author = "Bruno Giardina and Paolo Ascenzi and Clementi, \{Maria Elisabetta\} and \{De Sanctis\}, Giampiero and Menico Rizzi and Massimo Coletta",

year = "1996",

doi = "10.1074/jbc.271.29.16999",

language = "English",

volume = "271",

pages = "16999--17001",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "29",

}

TY - JOUR

T1 - Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein

AU - Giardina, Bruno

AU - Ascenzi, Paolo

AU - Clementi, Maria Elisabetta

AU - De Sanctis, Giampiero

AU - Rizzi, Menico

AU - Coletta, Massimo

PY - 1996

Y1 - 1996

N2 - The effect of lactate on O2 binding properties of sperm whale and horse heart myoglobins (Mb) has been investigated at moderately acid pH (i.e. pH 6.5, a condition which may be achieved in vivo under a physical effort). Addition of lactate brings about a decrease of O2 affinity (i.e. an increase of P50) in sperm whale and horse heart myoglobins. Accordingly, lactate shows a different affinity for the deoxygenated and oxygenated form, behaving as a heterotropic modulator. The lactate effect on O2 affinity appears to differ for sperm whale and horse heart Mb, δlogP50 being ≃1.0 and ≃0.4, respectively. From the kinetic viewpoint, the variation of O2 affinity for both myoglobins can be attributed mainly to a decrease of the kinetic association rate constant for ligand binding.

AB - The effect of lactate on O2 binding properties of sperm whale and horse heart myoglobins (Mb) has been investigated at moderately acid pH (i.e. pH 6.5, a condition which may be achieved in vivo under a physical effort). Addition of lactate brings about a decrease of O2 affinity (i.e. an increase of P50) in sperm whale and horse heart myoglobins. Accordingly, lactate shows a different affinity for the deoxygenated and oxygenated form, behaving as a heterotropic modulator. The lactate effect on O2 affinity appears to differ for sperm whale and horse heart Mb, δlogP50 being ≃1.0 and ≃0.4, respectively. From the kinetic viewpoint, the variation of O2 affinity for both myoglobins can be attributed mainly to a decrease of the kinetic association rate constant for ligand binding.

UR - https://www.scopus.com/pages/publications/0030015632

U2 - 10.1074/jbc.271.29.16999

DO - 10.1074/jbc.271.29.16999

M3 - Article

SN - 0021-9258

VL - 271

SP - 16999

EP - 17001

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 29

ER -

Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein

Abstract

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