Reaction of azide radicals with amino acids and proteins.
Int J Radiat Biol Relat Stud Phys Chem Med
; 36(1): 75-83, 1979 Jul.
Article
en En
| MEDLINE
| ID: mdl-40916
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Azidas
/
Proteínas
/
Radicales Libres
/
Aminoácidos
Idioma:
En
Revista:
Int J Radiat Biol Relat Stud Phys Chem Med
Año:
1979
Tipo del documento:
Article