Abstract
Proteus vulgaris and P. mirabilis were grown anaerobically on glucose in the absence or presence of dimethylsulphoxide (DMSO) as electron acceptor or on (S)- or (RS)-lactate in the presence of nitrogen (N)-oxides, sulphur (S)-oxides or pyruvate. During growth on glucose the main fermentation product was ethanol and in the presence of DMSO it was (R)-lactate. Growth on (RS)-lactate led to acetate and (R)-lactate and growth on (S)-lactate produced almost only acetate. Depending on the growth medium, in crude extracts of P. vulgaris the activities of (R)-2-hydroxycarboxylate viologen oxidoreductase (HVOR), measured as (R)-lactate dehydrogenase, and DMSO reductase were 0.5–8.0 and 0.3–1.1 units (U)/mg protein, respectively. Addition of nitrate to the growth medium diminished both enzyme activities to <0.1 U/mg protein. P. mirabilis showed also high HVOR activity when grown on (RS)-lactate in the presence of DMSO. Also, Clostridium homopropionicum contained 1.8 U/mg of a pyridine-nucleotide-independent reversible (R)-lactate dehydrogenase when tested with the electron acceptor 1,1′-carbomoylmethylviologen (NH2CO-MV). None of the organisms studied were significantly active with (S)-lactate and NH2CO-MV. The possible physiological role of the HVOR may be as a dissimilatory (R)-lactate dehydrogenase.
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References
Clark DP (1989) The fermentation pathways of Escherichia coli. FEMS Microbiol Rev 63:223–234
Dörner C, Schink B (1990) Clostridium homopropionicum sp. nov., a new strict anaerobe growing with 2-, 3-, or 4-hydroxybutyrate. Arch Microbiol 154:342–348
DSM (1989) Catalogue of strains German Collection of Microorganisms and Cell Cultures, Braunschweig
Fraisse L, Simon H (1988) Observations on the reduction of non-activated carboxylates by Clostridium formicoaceticum with carbon monoxide or formate and the influence of various viologens. Arch Microbiol 150:381–386
Gawehn K (1984) d-(—)-Lactate. In: Bergmeyer HU (ed) Methods of enzymatic analysis, vol 6, 3rd edn. Verlag Chemie, Weinheim, pp 588–592
Günther H, Neumann S, Simon H (1987) 2-Oxocarboxylate reductase from Proteus species and its use for the preparation of (2R)-hydroxy acids. J Biotechnol 5:53–65
Hummel W, Kula MR (1989) Dehydrogenases for the synthesis of chiral compounds. Eur J Biochem 184:1–13
Kallwass KW (1992) Potential of R-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei for stereospecific reductions. Enzyme Microb Technol 14:28–35
Kim MJ, Whitesides GM (1988) L-Lactate dehydrogenase: substrate specificity and the use as a catalyst in the synthesis of homochiral 2-hydroxy acids. J Am Chem Soc 110:2959–2964
Kröger A (1974) Electron-transport phosphorylation coupled to fumarate reduction in anaerobically grown Proteus rettgeri. Biochim Biophys Acta 347:273–289
Kunst A, Draeger B, Ziegenhorn J (1984) d-Glucose. In: Bergmeyer HU (ed) Methods of enzymatic analysis, vol 6, 3rd edn. Verlag Chemie, Weinheim, pp 163–172
Lamprecht W, Heinz F (1984) Pyruvate. In: Bergmeyer HU (ed) Methods of enzymatic analysis, vol 6, 3rd edn. Verlag Chemie, Weinheim, pp 570–577
Molinari R, Lara FJS (1960) The lactic dehydrogenase of Propionibacterium pentosaceum. Biochem J 75:57–66
Neumann S, Simon H (1984) On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad substrate specificity from two Proteus species. FEBS 167:29–32
Ogata M, Arikara K, Yagi T (1981) d-Lactate dehydrogenase of Desulfovibrio vulgaris. J Biochem 89:1423–1431
Read SM, Northcote DH (1981) Minimization of variation in the response to different proteins of the Coomassie blue G dye-binding assay for protein. Anal Biochem 116:53–64
Schaller KH, Triebig G (1984) Determination with formate dehydrogenase. In: Bergmeyer HU (ed) Methods of enzymatic analysis, vol 6, 3rd edn. Verlag Chemie, Weinheim, pp 668–672
Schinschel C (1992) Verfahren zur präparativen Darstellung von Pyruvat aus d-Lactat mit Proteus vulgaris. PhD Thesis, Technical University, Munich
Schummer A, Yu H, Simon H (1991) Polyfunctional (R)-2-hydroxycarboxylic acids by reduction of 2-oxo acids with hydrogen gas or formate and resting cells of Proteus vulgaris. Tetrahedron 47:9019–9034
Skopan H, Günther H, Simon H (1987) A biocatalyst for the preparation of (R)- and (S)-hydroxycarboxylic acids. Angew Chem Int Ed Engl 26:128–130
Srinivas SP, Rao G, Mutharasan R (1988) Redox potential in anaerobic and microaerobic fermentation. In: Erickson LE, Fung DYC (eds) Handbook on anaerobic fermentation. Dekker, New York, pp 147–186
Styrvold OB, Strøm AR (1984) Dimethylsulphoxide and trimethylamine oxide respiration of Proteus vulgaris. Arch Microbiol 140:74–78
Taguchi H, Ohta T (1991) d-Lactate dehydrogenase is a member of the d-isomer-specific 2-hydroxyacid dehydrogenase family. J Biol Chem 266:12588–12594
Tarbell DS, Weaver C (1941) The condensation of sulfoxides with p-toluenesulfonamide and substituted acetamides. J Am Chem Soc 63:2939–2942
Thanos I, Bader J, Günther H, Neumann S, Krauss F, Simon H (1987) Electroenzymatic and electromicrobial reduction: Preparation of chiral compounds. Methods Enzymol 136:302–317
Valentine-Serano A, Hudspeth MES, Meganathan R (1991) Reduction of N-oxides and sulfoxide by the same terminal reductase in Proteus mirabilis. Curr Microbiol 23:271–276
Zinder SH, Brock TD (1978) Dimethylsulfoxide as an electron acceptor for the anaerobic growth. Arch Microbiol 116:35–40
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Schinschel, C., Simon, H. Effect of carbon sources and electron acceptors in the growth medium of Proteus spp. on the formation of (R)-2-hydroxycarboxylate viologen oxidoreductase and dimethylsulphoxide reductase. Appl Microbiol Biotechnol 38, 531–536 (1993). https://doi.org/10.1007/BF00242950
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DOI: https://doi.org/10.1007/BF00242950