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dc.contributor.authorLand, Edward J
dc.contributor.authorPrütz, W
dc.date.accessioned2011-07-12T11:10:14Z
dc.date.available2011-07-12T11:10:14Z
dc.date.issued1979-07
dc.identifier.citationReaction of azide radicals with amino acids and proteins. 1979, 36 (1):75-83 Int J Radiat Biol Relat Stud Phys Chem Meden
dc.identifier.issn0020-7616
dc.identifier.pmid40916
dc.identifier.doi10.1080/09553007914550831
dc.identifier.urihttp://hdl.handle.net/10541/135876
dc.description.abstractThe azide radical N3 reacts selectively with amino acids, in neutral solution preferentially with tryptophan (k (N3 + TrpH) = 4.1 X 10(9) dm3 mol(-1s-1) and in alkaline solution also with cysteine and tyrosine (k(N3 + CyS-) = 2.7 X 10(9) dm3 mol-1s-1) and k(N3 + TyrO-) equals 03.6 X 10(9) dm3 mol-1s-1). Oxidation of the enzyme yADH by N3 involves primary attacks, mainly at tryptophan residues, and subsequent slow secondary reactions. N3-induced inactivation of yADH is likely to occur upon oxidation of tryptophan residues in the substrate binding pocket (58-TrpH and 93-TrpH) since the substrate ethanol although unreactive with N3, protects yADH and since elADH, which does not contain tryptophan in the substrate pocket, is comparatively resistant against N3-attack. N3 exhibits low reactivity with nucleic acid derivatives and it is inert towards aliphatic compounds such as methanol and sodium dodecylsulphate.
dc.language.isoenen
dc.subject.meshAlcohol Oxidoreductases
dc.subject.meshAmino Acids
dc.subject.meshAzides
dc.subject.meshEnzyme Activation
dc.subject.meshFree Radicals
dc.subject.meshHydrogen-Ion Concentration
dc.subject.meshKinetics
dc.subject.meshProteins
dc.subject.meshPulse Radiolysis
dc.titleReaction of azide radicals with amino acids and proteins.en
dc.typeArticleen
dc.contributor.departmentPaterson Laboratories, Christie Hospital and Holt Radium Institute, Manchesteren
dc.identifier.journalInternational journal of radiation biology and related studies in physics, chemistry, and medicineen
html.description.abstractThe azide radical N3 reacts selectively with amino acids, in neutral solution preferentially with tryptophan (k (N3 + TrpH) = 4.1 X 10(9) dm3 mol(-1s-1) and in alkaline solution also with cysteine and tyrosine (k(N3 + CyS-) = 2.7 X 10(9) dm3 mol-1s-1) and k(N3 + TyrO-) equals 03.6 X 10(9) dm3 mol-1s-1). Oxidation of the enzyme yADH by N3 involves primary attacks, mainly at tryptophan residues, and subsequent slow secondary reactions. N3-induced inactivation of yADH is likely to occur upon oxidation of tryptophan residues in the substrate binding pocket (58-TrpH and 93-TrpH) since the substrate ethanol although unreactive with N3, protects yADH and since elADH, which does not contain tryptophan in the substrate pocket, is comparatively resistant against N3-attack. N3 exhibits low reactivity with nucleic acid derivatives and it is inert towards aliphatic compounds such as methanol and sodium dodecylsulphate.


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