1887

Abstract

Summary: Enzyme determinations in bacteria-free extracts and dual-wavelength experiments with membrane suspensions established that converted glycerol into triose phosphate via glycerol kinase and NAD-independent glycerol 1-phosphate dehydrogenase which is closely linked to cytochrome Glycerol 1-phosphate dehydrogenase uses fumarate as a final hydrogen acceptor. The enzyme system catalysing fumarate reduction with glycerol 1-phosphate as a hydrogen donor, is membrane bound and is strongly inhibited by 2--heptyl-4-hydroxyquinoline-N-oxide (HOQNO). Fumarate reduction with reduced benzyl-viologen is not inhibited by HOQNO. Cytochrome is therefore probably involved in the anaerobic electron transport from glycerol 1-phosphate to fumarate. Molar growth yields and fermentation balances were determined for and growing on glucose, fructose, glycerol and lactate and ATP yields (mol of ATP formed/mol of substrate fermented) were calculated assuming that 1 mol ATP is formed in the electron transport from glycerol 1-phosphate and lactate to fumarate, and that 2 mol ATP are formed in the electron transport from NADH to fumarate. Mean values (g dry wt bacteria/mol ATP) were 15·2 and 12·9 for , and 16·4 and 11·8 for each growing on complex or synthetic medium respectively. The observation that for each strain Y values were constant for the same medium, supported our assumptions on energy generation in propionic acid bacteria.

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/content/journal/micro/10.1099/00221287-76-1-31
1973-05-01
2019-10-17
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-76-1-31
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