LINKAGE OF FORMATE HYDROGENLYASE WITH ANAEROBIC RESPIRATION IN PROTEUS-MIRABILIS
LINKAGE OF FORMATE HYDROGENLYASE WITH ANAEROBIC RESPIRATION IN PROTEUS-MIRABILIS
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DOI:
10.1016/0005-2728(82)90254-7
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发表时间:
1982-01-01
期刊:
影响因子:
--
通讯作者:
STOUTHAMER, AH
中科院分区:
文献类型:
--
作者:
KRAB, K;OLTMANN, LF;STOUTHAMER, AH
The linkage between the enzyme system catalyzing formate hydrogenlyase and reductases involved in anaerobic respiration in intact cells of anaerobically grown P. mirabilis was studied. Reduction of nitrate and fumarate by H2 or formate was possible under all growth conditions; reduction of tetrathionate and thiosulfate occurred only in cells harvested at late growth phase from a pH-regulated batch culture and not in cells harvested at early growth phase or in cells grown in pH-auxostat culture. Under all conditions, cells possessed the enzyme tetrathionate reductase. Linkage between tetrathionate reductase (catalyzing also reduction of thiosulfate) and the formate hydrogenlyase chain is dependent on growth conditions. During reduction of high-potential oxidants such as fumarate, tetrathionate (when possible) or the artificial electron acceptor methylene blue by formate, there was no simultaneous H2 evolution due to the formate hydrogenlyase reaction. H2 production started only after complete reduction of methylene blue or fumarate, in the case of methylene blue after a lag phase without gas production. In preparations with a low fumarate reduction activity this was accompanied by an acceleration in CO2 production. During reduction of thiosulfate (a low-potential oxidant) or of tetrathionate in the presence of benzyl viologen (a low-potential mediator) by formate, H2 was evolved simultaneously. Formate hydrogenlyase is apparently regulated by a factor that responds to the redox state of any electron acceptor couple present such that lyase activity is blocked when the acceptor couple is oxidized to too great an extent.