Reaction of azide radicals with amino acids and proteins.
dc.contributor.author | Land, Edward J | |
dc.contributor.author | Prütz, W | |
dc.date.accessioned | 2011-07-12T11:10:14Z | |
dc.date.available | 2011-07-12T11:10:14Z | |
dc.date.issued | 1979-07 | |
dc.identifier.citation | Reaction of azide radicals with amino acids and proteins. 1979, 36 (1):75-83 Int J Radiat Biol Relat Stud Phys Chem Med | en |
dc.identifier.issn | 0020-7616 | |
dc.identifier.pmid | 40916 | |
dc.identifier.doi | 10.1080/09553007914550831 | |
dc.identifier.uri | http://hdl.handle.net/10541/135876 | |
dc.description.abstract | The 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.iso | en | en |
dc.subject.mesh | Alcohol Oxidoreductases | |
dc.subject.mesh | Amino Acids | |
dc.subject.mesh | Azides | |
dc.subject.mesh | Enzyme Activation | |
dc.subject.mesh | Free Radicals | |
dc.subject.mesh | Hydrogen-Ion Concentration | |
dc.subject.mesh | Kinetics | |
dc.subject.mesh | Proteins | |
dc.subject.mesh | Pulse Radiolysis | |
dc.title | Reaction of azide radicals with amino acids and proteins. | en |
dc.type | Article | en |
dc.contributor.department | Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester | en |
dc.identifier.journal | International journal of radiation biology and related studies in physics, chemistry, and medicine | en |
html.description.abstract | The 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. |