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Literature DB >> 6852193

Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin.

F Tursi, M Samaia, M Salmona, G Belvedere.

Abstract

Oxygenated human erythrocytes catalyzed the oxidation of styrene to styrene oxide. This reaction was inhibited by CO but not by superoxide dismutase, catalase and scavengers of hydroxyl radicals. In partially deoxygenated erythrocytes styrene oxidation showed a linear relationship with the molar fraction of oxyhemoglobin. These data indicate that oxyhemoglobin and not free oxygen radicals are involved in styrene oxidation.

Entities: Chemical Gene Species

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Year: 1983 PMID： 6852193 DOI： 10.1007/bf01971112

Source DB: PubMed Journal: Experientia ISSN： 0014-4754

28 in total

1. NATURE OF THE IRON-OXYGEN BOND IN OXYHAEMOGLOBIN.

Authors: J J WEISS
Journal: Nature Date: 1964-04-04 Impact factor: 49.962

2. Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex.

Authors: J M McCord; E D Day
Journal: FEBS Lett Date: 1978-02-01 Impact factor: 4.124

3. Simultaneous determination of hemoglobin derivatives, oxygen content, oxygen capacity, and oxygen saturation in 10 microliters of whole blood.

Authors: L Rossi-Bernardi; M Perella; M Luzzana; M Samaja; I Raffaele
Journal: Clin Chem Date: 1977-07 Impact factor: 8.327

4. The generation of superoxide radical during the autoxidation of hemoglobin.

Authors: H P Misra; I Fridovich
Journal: J Biol Chem Date: 1972-11-10 Impact factor: 5.157

5. A mechanism for the production of ethylene from methional. The generation of the hydroxyl radical by xanthine oxidase.

Authors: C Beauchamp; I Fridovich
Journal: J Biol Chem Date: 1970-09-25 Impact factor: 5.157

10. Generation of hydroxyl radical by enzymes, chemicals, and human phagocytes in vitro. Detection with the anti-inflammatory agent, dimethyl sulfoxide.

Authors: J E Repine; J W Eaton; M W Anders; J R Hoidal; R B Fox
Journal: J Clin Invest Date: 1979-12 Impact factor: 14.808

1 in total

1. The Redox Potential of the β-⁹³-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments.

Authors: Federico Maria Rubino
Journal: Molecules Date: 2021-04-26 Impact factor: 4.411

1 in total

Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin.

1. NATURE OF THE IRON-OXYGEN BOND IN OXYHAEMOGLOBIN.

2. Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex.

3. Simultaneous determination of hemoglobin derivatives, oxygen content, oxygen capacity, and oxygen saturation in 10 microliters of whole blood.

4. The generation of superoxide radical during the autoxidation of hemoglobin.

5. A mechanism for the production of ethylene from methional. The generation of the hydroxyl radical by xanthine oxidase.

6. Effect of iron and hemoproteins on hydrogen peroxide-supported styrene oxidation to styrene oxide.

7. Microsomal styrene mono-oxygenase and styrene epoxide hydrase activities in rats.

8. Enhancement of hexose uptake in human polymorphonuclear leukocytes by activated complement component C5a.

9. Styrene oxidation to styrene oxide in human blood erythrocytes and lymphocytes.

10. Generation of hydroxyl radical by enzymes, chemicals, and human phagocytes in vitro. Detection with the anti-inflammatory agent, dimethyl sulfoxide.

1. The Redox Potential of the β-⁹³-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments.