Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 480, Issue 1, Pages 33-40Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.09.003
Keywords
Chloroperoxidase; CYP; Enzymatic kinetics; Docking calculations; pi-pi dinners; PAH
Categories
Funding
- Instituto Mexicano del Petroleo [D.00023/293]
- PROMEP [47410065]
- COFAA-SIP/ IPN [20080026]
- Faculty of Medicine, UNAM)
Ask authors/readers for more resources
We have identified an atypical kinetic behavior for the oxidative halogenation of several polycyclic aromatic hydrocarbons (PAHs) by chloroperoxidase (CPO) from Caldariomyces fumago. This behavior resembles the capacity of some members of the P450 family to simultaneously recognize several substrate molecules at their active sites. Indeed, fluorometric studies showed that PAHs exist in solution as monomers and pi-pi dimers that interact to different extents with CPO. The dissociation constants of dimerization were evaluated for every single PAH by spectrofluorometry. Furthermore, docking studies also suggest that CPO might recognize either one or two substrate molecules in its active site. The atypical sigmoidal kinetic behavior of CPO in the oxidative halogenation of PAHs is explained in terms of different kinetic models for non-heteroatomic PAHs (naphthalene, anthracene and pyrene). The results suggest that the actual substrate for CPO in this study was the pi-pi dimer for all evaluated PAHs. (C) 2008 Elsevier Inc. All rights reserved
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available