Near stoichiometric, irreversible inactivation of bacterial collagenases by o-chloranil (3,4,5,6-tetrachloro-1,2-benzoquinone).
The hydrogen-abstracting quinone derivative 3,4,5,6-tetrachloro-1,2-benzoquinone (o-chloranil) caused a strong, near stoichiometric, irreversible inactivation of the collagenases from Bacillus cereus, Clostridium histolyticum and Achromobacter iophagus. p-Chloranil was a weaker inactivator. o-Chloranil reacted rapidly with a site that affected substrate binding. Amino acid analyses of native and totally inactivated enzymes, and the pH-profile of inactivation suggest that the dissociated form of a tyrosine residue was modified.
Makinen
P L
PL
Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor 48109.
Makinen
K K
KK
D000421:Alcaligenes / Q000201:enzymology*; D001409:Bacillus cereus / Q000201:enzymology*; D002703:Chloranil / Q000031:analogs & derivatives / Q000494:pharmacology*; D003013:Clostridium / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007536:Isomerism; D007700:Kinetics; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors*; D011809:Quinones / Q000494:pharmacology*; D013053:Spectrophotometry
D011809:Quinones; D002703:Chloranil; D003012:Microbial Collagenase; C039499:2-chloranil