ISSN:
1432-072X
Keywords:
Clostridium sp. La 1
;
Carbon sources
;
Clostridium kluyveri
;
Hydrogenase
;
Enoate reductase
;
Relationship of enoate reductase and hydrogenase
;
Iron
;
Sulfur
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The enzyme activities of Clostridium La 1 and Clostridium kluyveri involved in the stereospecific hydrogenation of α,β-unsaturated carbonyl compounds with hydrogen gas were measured. In C. La 1 the specific activities of hydrogenase and enoate reductase depended heavily on the growth phase and the composition of the medium. During growth in batch cultures on 70 mM crotonate the specific activity of hydrogenase increased and then dropped to about 10% of its maximum value, whereas the activity of enoate reductase reached its maximum in cells of the stationary phase. Under certain conditions during growth the activity ratio hydrogenase: enoate reductase changed from 120 to 1. Thus, the rate limiting enzyme for the hydrogenation can be either the hydrogenase or the enoate reductase, depending on the growth conditions of the cells. The specific activities of ferredoxin-NAD reductase and butyryl-CoA dehydrogenase increased 3-4-fold during growth on crotonate. By turbidostatic experiments it was shown that at constant input of high crotonate concentrations (200 mM) the enoate reductase activity was almost completely suppressed; it increased steadily with decreasing crotonate down to an input concentration of 35 mM. Glucose as carbon source led to high hydrogenase and negligible enoate reductase activities. The latter could be induced by changing the carbon source of the medium from glucose to crotonate. Tetracycline inhibited the formation of enoate reductase. A series of other carbon sources was tested. They can be divided into ones which result in high hydrogenase and rather low enoate reductase activities and others which cause the reverse effect. When the Fe2+ concentration in crotonate medium was growth limiting, cells with relatively high hydrogenase activity and very low enoate reductase activity in the stationary phase were obtained. At Fe2+ concentrations above 3·10-7 M enoate reductase increased and hydrogenase activity reached its minimum. The ratio of activities changes by a factor of about 200. In a similar way the dependence of enzyme activities on the concentration of sulfate was studied. In batch cultures of Clostridium kluyveri a similar opposite time course of enoate reductase and hydrogenase was found. The possible physiological significance of this behavior is discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00427205
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