Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover

scientific article published on 01 February 1997

Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1021/BI961868Y
P698PubMed publication ID9048579

P2093author name stringProfumo A
Casella L
Monzani E
Gullotti M
Gatti AL
P2860cites workPhysical and compositional investigations of the subfractions of lactoperoxidaseQ72414218
P433issue7
P407language of work or nameEnglishQ1860
P304page(s)1918-1926
P577publication date1997-02-01
P1433published inBiochemistryQ764876
P1476titleOxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover
P478volume36

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cites work (P2860)
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Q30731693Binding and relaxometric properties of heme complexes with cyanogen bromide fragments of human serum albumin
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Q48362724Enhancing hypothiocyanite production by lactoperoxidase - mechanism and chemical properties of promotors
Q43643301Enzymatic properties of human hemalbumin
Q24812367Formation of reactive nitrogen species at biologic heme centers: a potential mechanism of nitric oxide-dependent toxicity
Q38295873Glu375Gln and Asp225Val mutants: about the nature of the covalent linkages between heme group and apo-Protein in bovine lactoperoxidase
Q59400065Kinetics and Thermodynamics of Halide and Nitrite Oxidation by Mammalian Heme Peroxidases
Q38139409Lactoperoxidase: structural insights into the function,ligand binding and inhibition.
Q27658143Mode of Binding of the Tuberculosis Prodrug Isoniazid to Heme Peroxidases: BINDING STUDIES AND CRYSTAL STRUCTURE OF BOVINE LACTOPEROXIDASE WITH ISONIAZID AT 2.7 A RESOLUTION
Q44523616Oxidation of mitoxantrone by lactoperoxidase.
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Q44593302Reactivity study on microperoxidase-8
Q42670367Single-site mutations on the catalase-peroxidase from Sinorhizobium meliloti: role of the distal Gly and the three amino acids of the putative intrinsic cofactor
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Q39907653Structural evidence for the order of preference of inorganic substrates in mammalian heme peroxidases: crystal structure of the complex of lactoperoxidase with four inorganic substrates, SCN, I, Br and Cl.
Q74223848Surfactant-lactoperoxidase complex catalytically active in organic media
Q35586114Unraveling the catalytic mechanism of lactoperoxidase and myeloperoxidase
Q42821682Uric acid and thiocyanate as competing substrates of lactoperoxidase

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