ISSN:
1432-072X
Keywords:
Desulfovibrio
;
Dicarboxylic acids
;
l-Malate
;
NADPH dehydrogenase
;
Dissimilatory sulfate reduction
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract Four out of five Desulfovibrio strains tested were able to oxidize l-malate to acetate in the presence of sulfate. Fumarate and succinate were also oxidized to acetate by these strains, but growth with the latter substrate was marginal. During growth on malate high NADP-dependent malic enzyme and NADPH DH activities were found in all strains. These activities were lower in lactate-or pyruvate-grown cells. An NADPH DH from D. gigas was partially purified. It was oxygen-labile, very sensitive to heavy metal ions and highly specific for NADPH. Growth yield studies indicated that energy conservation occurred during the transport of reducing equivalents from NADPH to the sulfate reduction pathway.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00444665
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