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Literature DB >> 14154472

STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. I. HUMAN HEMOGLOBIN.

E ANTONINI, J WYMAN, M BRUNORI, J F TAYLOR, A ROSSI-FANELLI, A CAPUTO.

Abstract

Entities: Disease Species

Keywords: EXPERIMENTAL LAB STUDY; HEMOGLOBIN; HYDROGEN-ION CONCENTRATION; OXIDATION-REDUCTION; OXYGEN; SPECTROPHOTOMETRY; TEMPERATURE

Mesh：

Substances：

Year: 1964 PMID： 14154472

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

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18 in total

1. Linearity of the hemoglobin oxidation bohr effect.

Authors: B M Hoffman; C Bull
Journal: Proc Natl Acad Sci U S A Date: 1976-03 Impact factor: 11.205

2. Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins.

Authors: Celia Bonaventura; Robert Henkens; Joel Friedman; Claire J Parker Siburt; Daniel Kraiter; Alvin L Crumbliss
Journal: Biochim Biophys Acta Date: 2011-07-08

3. Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control.

Authors: Zhi Huang; Sruti Shiva; Daniel B Kim-Shapiro; Rakesh P Patel; Lorna A Ringwood; Cynthia E Irby; Kris T Huang; Chien Ho; Neil Hogg; Alan N Schechter; Mark T Gladwin
Journal: J Clin Invest Date: 2005-07-21 Impact factor: 14.808

4. Cooperative free energies for nested allosteric models as applied to human hemoglobin.

Authors: S J Gill; C H Robert; M Coletta; E Di Cera; M Brunori
Journal: Biophys J Date: 1986-10 Impact factor: 4.033

5. Kinetics of the reaction of the sulphydryl groups of human hemoglobin and globin with para-mercuribenzoate in alkaline solution.

Authors: D L Currell; C Ioppolo
Journal: Experientia Date: 1974-12-15

STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. I. HUMAN HEMOGLOBIN.

1. Linearity of the hemoglobin oxidation bohr effect.

2. Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins.

3. Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control.

4. Cooperative free energies for nested allosteric models as applied to human hemoglobin.

5. Kinetics of the reaction of the sulphydryl groups of human hemoglobin and globin with para-mercuribenzoate in alkaline solution.

6. Subunit exchange and ligand binding: a new hypothesis for the mechanism of oxygenation of hemoglobin.

7. Conversion of oxyhaemoglobin into methaemoglobin by ferricytochrome b5.

8. The effect of ligand on the kinetics of the sulfhydryl groups of human hemoglobin with p-mercuribenzoate.

9. Oxidation of nicotinamide coenzyme dimers by one-electron-accepting proteins.

10. The interaction of inositol hexaphosphate with methaemoglobin.