Characterization of radicals in anaerobic degradation of benzoate, acytelene, and glycol ethers

Applicant Professor Dr. Bernhard Schink
Subject Area Metabolism, Biochemistry and Genetics of Microorganisms
Term from 1999 to 2007
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 5177536
 

Project Description

In fermenting and sulfate-reducing bacteria, the reductive transformation of benzoyl-CoA is catalyzed by an enzyme system different from that observed in nitrate-reducing bacteria. The reaction leads to cyclohexene carboxyl-CoA, and appears to be ATP-independent. Formation of a radical carbonyl derivative is proposed for the first step which is subsequently reduced to cyclohexene carboxyl-CoA. A second project deals with the fermentative degradation of ethylene glycol ethers which is supposed to proceed via a radical mechanism analogous to the reaction catalyzed by diol dehydratases. In a third project, the molybdopterin-containing enzyme acetylene hydratase will be investigated with respect to the formation of a pterin-centered radical and its role in catalysis. Clearly, in all cases protein and substrate centered radicals will be identified by EPR/ENDOR spectroscopy employing both rapid quench and spin trap techniques.
DFG Programme Priority Programmes
Subproject of SPP 1071:  Radikale in der enzymatischen Katalyse
Participating Person Professor Dr. Peter M. H. Kroneck