Literature DB >> 24226548

Generation of hydroxyl radicals by soybean nodule leghaemoglobin.

A Puppo1, B Halliwell.   

Abstract

Leghaemoglobin, a protein present in root nodules of soybean (Glycine max (L.) Merr.), generates the highly reactive hydroxyl radical (·OH) upon incubation with hydrogen peroxide (H2O2). The H2O2 appears to cause breakdown of the haem, releasing iron ions that convert H2O2 into ·OH outside the protein. Oxyleghaemoglobin (oxygenated ferrous protein) is more sensitive to attack by H2O2 than is metleghaemoglobin (ferric protein). The possibility of oxyleghaemoglobin breakdown by H2O2 and formation of damaging ·OH may explain why the root nodule is equipped with iron-storage proteins and enzymes that can remove H2O2.

Entities:  

Year:  1988        PMID: 24226548     DOI: 10.1007/BF00401028

Source DB:  PubMed          Journal:  Planta        ISSN: 0032-0935            Impact factor:   4.116


  24 in total

1.  The absence of oxidized leghemoglobin in soybean root nodules during nodule development.

Authors:  D T Nash; H M Schulman
Journal:  Biochem Biophys Res Commun       Date:  1976-02-09       Impact factor: 3.575

Review 2.  The measurement of free radical reactions in humans. Some thoughts for future experimentation.

Authors:  B Halliwell; M Grootveld
Journal:  FEBS Lett       Date:  1987-03-09       Impact factor: 4.124

3.  Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates: is it a mechanism for hydroxyl radical production in biochemical systems?

Authors:  B Halliwell
Journal:  FEBS Lett       Date:  1978-08-15       Impact factor: 4.124

Review 4.  The importance of free radicals and catalytic metal ions in human diseases.

Authors:  B Halliwell; J M Gutteridge
Journal:  Mol Aspects Med       Date:  1985

5.  Formation of thiobarbituric-acid-reactive substance from deoxyribose in the presence of iron salts: the role of superoxide and hydroxyl radicals.

Authors:  B Halliwell; J M Gutteridge
Journal:  FEBS Lett       Date:  1981-06-15       Impact factor: 4.124

6.  The reaction of ferrous leghemoglobin with hydrogen peroxide to form leghemoglobin(IV).

Authors:  I Aviram; A Wittenberg; J B Wittenberg
Journal:  J Biol Chem       Date:  1978-08-25       Impact factor: 5.157

7.  Inhibition of the iron-catalysed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine.

Authors:  J M Gutteridge; R Richmond; B Halliwell
Journal:  Biochem J       Date:  1979-11-15       Impact factor: 3.857

8.  Hemoglobin. A biologic fenton reagent.

Authors:  S M Sadrzadeh; E Graf; S S Panter; P E Hallaway; J W Eaton
Journal:  J Biol Chem       Date:  1984-12-10       Impact factor: 5.157

9.  Study of the pseudoperoxidatic activity of soybean leghemoglobin and sperm whale myoglobin.

Authors:  G Sievers; M Rönnberg
Journal:  Biochim Biophys Acta       Date:  1978-04-26

10.  Possible involvement of nodule superoxide dismutase and catalase in leghemoglobin protection.

Authors:  A Puppo; L Dimitrijevic; J Rigaud
Journal:  Planta       Date:  1982-12       Impact factor: 4.116

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  2 in total

1.  Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity.

Authors:  Ullas Valiya Chembazhi; Vinod Vikas Patil; Shivjee Sah; Wayne Reeve; Ravi P Tiwari; Euijeon Woo; Umesh Varshney
Journal:  Nucleic Acids Res       Date:  2017-06-02       Impact factor: 16.971

2.  Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress.

Authors:  Olga V Kosmachevskaya; Elvira I Nasybullina; Konstantin B Shumaev; Alexey F Topunov
Journal:  Molecules       Date:  2021-11-28       Impact factor: 4.411

  2 in total

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