Abstract
The primary reaction in the degradation of n-alkane-1-sulfonates by Pseudomonas is the hydroxylation of the carbon atom bearing the sulfonate group. The 1-hydroxy-n-alkane-1-sulfonate (aldehyde-bisulfite adduct) formed easily hydrolyses to give the corresponding aldehyde and bisulfite.
The enzyme catalysing the hydroxylation reaction depends for its action on the presence of molecular oxygen and NADH. The kinetics of this reaction and the substrate specificity of the enzyme were studied using a crude enzyme extract and a spectrophotometric assay method based on co-oxidation of NADH with the sulfonate.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Conrad, H. E., DuBus, R. and Gunsalus, I. C. 1961. An enzyme system for cyclic ketene lactonization. — Biochem. Biophys. Res. Commun. 6: 293–297.
Dixon, M. and Webb, E. C. 1964. Enzymes, 2nd ed. p. 75. — Longmans, Green and Co. Ltd. London, New York, Toronto.
Fieser, L. F. and Fieser, M. 1959. Basic organic chemistry, p. 192. — D. C. Heath and Comp., Boston.
Focht, D. D. and Williams, F. D. 1970. The degradation of p-toluenesulfonate by a Pseudomonas. — Can. J. Microbiol. 16: 309–316.
Forney, F. W. and Markovetz, A. J. 1969. An enzyme system for aliphatic methyl ketone oxidation. — Biochem. Biophys. Res. Comm. 37: 31–38.
Horvath, R. S. and Koft, B. W. 1972. Degradation of alkyl benzene sulfonate by Pseudomonas species. — Appl. Microbiol. 23: 407–414.
Van der Linden, A. C. and Huybregtse, R. 1969. Occurrence of inducible and NAD(P)-independent primary alcohol dehydrogenases in an alkane-oxidizing Pseudomonas. —Antonie van Leeuwenhoek 35: 344–360.
Lowry, O. H., Rosebourgh, N. J., Farr, A. L. and Randall, R. J. 1951. Protein measurement with the Folin phenol reagent. — J. Biol. Chem. 193: 265–275.
Martelli, H. L. and Souza, S. M. 1970. Biochemistry of sulfonic compounds. III. Formation of a two-carbon compound during the oxidation of sulfoacetate by a Pseudomonas strain. —Biochim. Biophys. Acta 208: 110–115.
Norris, D. B. and Trudgill, P. W. 1971. The metabolism of cyclohexanol by Nocardia globerula CL 1. — Biochem. J. 121: 363–370.
Van Ravenswaay Claasen, J. C. and Van der Linden, A. C. 1971. Substrate specificity of the paraffin hydroxylase of Pseudomonas aeruginosa. — Antonie van Leeuwenhoek 37: 339–352.
Thysse, G. J. E. and Wanders, T. H. 1972. Degradation of n-alkane-1-sulfonates by Pseudomonas. — Antonie van Leeuwenhoek 38: 53–63.
Umbreit, W. W., Burris, R. H. and Stauffer, J. F. 1972. Manometric and biochemical techniques, 5th ed., p. 291–294. — Burgess Publ. Co., Minneapolis.
West, P. W. and Gaeke, G. C. 1956. Fixation of sulfur dioxide as disulfitomercurate (II) and subsequent colorimetric estimation. — Anal. Chem. 28: 1816–1819.
Willetts, A. J. and Cain, R. B. 1972. Microbial metabolism of alkylbenzene sulphonates. Bacterial metabolism of undecylbenzene-p-sulphonate and dodecylbenzene-p-sulphonate. — Biochem. J. 129: 389–402.
Yano, I., Furukawa, Y. and Kusunose, M. 1971. α-Oxidation of long-chain fatty acids in cell-free extracts of Arthrobacter simplex. — Biochim. Biophys. Acta 239: 513–516.
Author information
Authors and Affiliations
Additional information
Shell Research B.V.
Rights and permissions
About this article
Cite this article
Thysse, G.J.E., Wanders, T.H. Initial steps in the degradation of n-alkane-1-sulphonates by Pseudomonas . Antonie van Leeuwenhoek 40, 25–37 (1974). https://doi.org/10.1007/BF00394550
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00394550