Allosteric properties of hemoglobin and the plasma membrane of the erythrocyte: new insights in gas transport and metabolic modulation.
Within the red blood cell the hemoglobin molecule is subjected to modulation mechanisms, namely homo- and heterotropic interactions, which optimize its functional behavior to the specific physiological requirements. At the cellular level, these modulation mechanisms are utilized to perform a number of other functions that are not minor with respect to the basic function of oxygen transport. Here we report some key examples concerning: (i) the interaction of hemoglobin with band 3 and its influence on glucose metabolism; (ii) the role of the ligand-linked quaternary transition of hemoglobin in the control of "NO bioactivity" and of gas diffusion; (iii) the interaction of plasma membrane with the various oxidative derivatives of the hemoglobin molecule.
De Rosa
Maria Cristina
MC
Institute of Biochemistry and Clinical Biochemistry, CNR Institute of Chemistry of Molecular Recognition, Catholic University of Rome, Rome, Italy.
Carelli Alinovi
Cristiana
C
Galtieri
Antonio
A
Russo
Annamaria
A
Giardina
Bruno
B
D019794:2,3-Diphosphoglycerate / Q000097:blood; D000494:Allosteric Regulation; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism; D001786:Blood Glucose / Q000378:metabolism; D004058:Diffusion; D004910:Erythrocyte Membrane / Q000502:physiology*; D005740:Gases / Q000097:blood; D006019:Glycolysis; D006454:Hemoglobins / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D046911:Macromolecular Substances / Q000378:metabolism; D010084:Oxidation-Reduction; D026403:S-Nitrosothiols / Q000097:blood
D001457:Anion Exchange Protein 1, Erythrocyte; D001786:Blood Glucose; D005740:Gases; D006454:Hemoglobins; D046911:Macromolecular Substances; D026403:S-Nitrosothiols; C103574:S-nitrosohemoglobin; D019794:2,3-Diphosphoglycerate