Inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase fromPseudomonas sp. strain CB406 by 3,4-dihydroxybiphenyl (4-phenylcatechol) |
| |
Authors: | Gareth Lloyd-Jones Richard C Ogden Peter A Williams |
| |
Institution: | (1) School of Biological Sciences, University of Wales, LL57 2UW Bangor, Gwynedd, U.K. |
| |
Abstract: | Summary 3,4-dihydroxybiphenyl is not a substrate for the 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) from biphenyldegradingPseudomonas sp. strain CB406. It acts as both a reversible inhibitor and a potent inactivator of the enzyme. The inactivation process requires the presence of O2 and can be reversed by the removal of the 3,4-dihydroxybiphenyl followed by incubation of the enzyme in the presence of dithioerythritol and Fe2+ under anaerobic conditions. Two other extradiol dioxygenases behave similarly, the catechol 2,3-dioxygenase (BphE) from strain CB406 and the BphC fromPseudomonas sp. strain LB400. The BphC fromP. testosteroni B-356 also did not cleave 3,4-dihydroxybiphenyl but it was not inactivated.Abbreviations C23o
Catechol 2,3-dioxygenase
- 34DHBP
3,4-dihydroxybiphenyl |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|