https://zenodo.org/record/1258475/files/article.pdf

Electron transfers in chemistry and biology

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Estimation of the molecular weights of proteins by Sephadex gel-filtration.

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

O2- oxidizes the [4Fe-4S] clusters of dehydratases, such as aconitase, causing-inactivation and release of Fe(II), which may then reduce H2O2 to OH- +OH.. SODs inhibit such HO. production by scavengingO2-, but Cu, ZnSODs, by virtue of a nonspecific peroxidase activity, may peroxidize spin trapping agents and thus give the appearance of catalyzing OH. production from H2O2. There is a glycosylated, tetrameric Cu, ZnSOD in the extracellular space that binds to acidic glycosamino-glycans. It minimizes the reaction of O2- with NO. E. coli, and other gram negative microorganisms, contain a periplasmic Cu, ZnSOD that may serve to protect against extracellular O2-. Mn(III) complexes of multidentate macrocyclic nitrogenous ligands catalyze the dismutation of O2- and are being explored as potential pharmaceutical agents. SOD-null mutants have been prepared to reveal the biological effects of O2-. SodA, sodB E. coli exhibit dioxygen-dependent auxotrophies and enhanced mutagenesis, reflecting O2(-)-sensitive biosynthetic pathways and DNA damage. Yeast, lacking either Cu, ZnSOD or MnSOD, are oxygen intolerant, and the double mutant was hypermutable and defective in sporulation and exhibited requirements for methionine and lysine. A Cu, ZnSOD-null Drosophila exhibited a shortened lifespan.

Superoxide Radical and Superoxide Dismutases

The reactive superoxide radical, O2-, formerly of concern only to radiation chemists and radiobiologists, is now understood to be a normal product of the biological reduction of molecular oxygen. An unusual family of enzymes, the superoxide dismutases, protect against the deleterious actions of this radical by catalyzing its dismutation to hydrogen peroxide plus oxygen.

https://science.sciencemag.org/content/sci/201/4359/875.full.pdf

The biology of oxygen radicals

Hemoglobin and myoglobin in their reactions with ligands

Studies on the oxygen and carbon monoxide equilibria of human myoglobin

Publisher Summary This chapter describes the procedures for the isolation of globin in the native state and for its reconstitution with metalloporphyrins. Globins are isolated from the corresponding hemoproteins by the removal of the heme moiety at acid pH, under controlled experimental conditions. The quality of the globin samples obtained can be checked by titration experiments with hemin (ferric protoheme) and by studying the properties of the reconstituted hemoproteins. There are two known methods for the preparation of globin from the holoprotein; both are based on the decreased affinity of the heme for globin at acid pH values. The first method employs acid–acetone at low temperature to split the heme group from the globin, which precipitates and is subsequently redissolved in water. A second method is based on heme extraction in methyl ethyl ketone at acid pH; in this case, the apoprotein remains dissolved in the aqueous layer. Further purification of the globin is accomplished similarly in both methods. The chapter presents the physicochemical properties of globin.

Preparation and properties of apohemoglobin and reconstituted hemoglobins.

Studies on the relations between molecular and functional properties of hemoglobin. I. The effect of salts on the molecular weight of human hemoglobin.

Eraldo Antonini

Papers

Hemoglobin and myoglobin in their reactions with ligands

Studies on the oxygen and carbon monoxide equilibria of human myoglobin

Preparation and properties of apohemoglobin and reconstituted hemoglobins.

Studies on the relations between molecular and functional properties of hemoglobin. I. The effect of salts on the molecular weight of human hemoglobin.

Studies on the functional properties of fish hemoglobins: II. The oxygen equilibrium of the isolated hemoglobin components from trout blood