Complete anaerobic oxidation of hydroquinone by Desulfococcus sp. strain Hy5: indications of hydroquinone carboxylation to gentisate
Author(s) -
Norbert Gorny,
Bernhard Schink
Publication year - 1994
Publication title -
archives of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.648
H-Index - 102
eISSN - 1432-072X
pISSN - 0302-8933
DOI - 10.1007/bf00264386
Subject(s) - hydroquinone , chemistry , strain (injury) , biochemistry , enzyme , anaerobic exercise , biology , anatomy , physiology
The sulfate-reducing strain Hy5 was able to grow with hydroquinone as sole source of carbon and energy. In experiments with dense cell suspensions, several indications were found that gentisate was the first intermediate in anaerobic degradation of hydroquinone: (1) degradation of hydroquinone was accelerated by addition of bicarbonate; (2) cell suspensions grown with hydroquinone oxidized gentisate at a rate similar to that of suspensions grown with gentisate, whereas the latter were not able to degrade hydroquinone in the presence of chloramphenicol; (3) in SDS-PAGE analysis of cell-free extracts of strain Hy5, two additional protein bands were found after growth with hydroquinone that were not detected in cells grown with gentisate, probably representing a hydroquinone carboxylating enzyme. A corresponding enzyme activity could not be detected. In cell-free extracts of hydroquinone-grown strain Hy5, the specific acyl-CoA ligase activity with gentisate as substrate was detected at 70 nmol x mg-1 x min-1. Gentisyl-CoA was enzymatically reduced to several unidentified nonaromatic products in the presence of dithionite-reduced methyl viologen.
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