Abstract
Catechol 1,2-dioxygenase has been purified 46-fold from cells of Rhizobium trifolii TA1 grown on benzoate plus glucose. The dioxygenase had a molecular weight of 107,000 and a sub-unit molecular weight of 59,000. The enzyme had a K m of 2 μM for catechol and also cleaved 4-methylcatechol. The dioxygenase contained 2 g atoms of Fe3+ per mole of enzyme which could be removed by treatment with 1,10-phenanthroline, resulting in a complete loss of activity; reactivation of the enzyme occurred specifically with Fe3+.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Brown CM, Dilworth MJ (1975) Ammonia assimilation by Rhizobium cultures and bacteroids. J Gen Microbiol 86:39–48
Chen YP, Glenn AR, Dilworth MJ (1984a) Uptake and oxidation of aromatic substrates by Rhizobium leguminosarum MNF 3841 and Rhizobium trifolii TA1. FEMS Microbiol Lett 21:201–205
Chen YP, Dilworth MJ, Glenn AR (1984b) Aromatic metabolism in Rhizobium trifolii— protocatechuate 3,4-dioxygenase. Arch Microbiol 138:187–190
Dilworth MJ, Glenn AR (1980) Control of carbon substrate utilization by rhizobia. In: Gibson AH, Newton WE (eds) Current perspectives in nitrogen fixation. Australian Academy of Sciences, Canberra, pp 244–251
Dilworth MJ, McKay I, Franklin MF, Glenn AR (1983) Catabolite effects on enzyme induction and substrate utilization in Rhizobium leguminosarum. J Gen Microbiol 122:61–67
Glenn AR, Dilworth MJ (1980) The effect of metal ions on the alkaline phosphatase of Rhizobium leguminosarum. Arch Microbiol 126:251–256
Glenn AR, Dilworth MJ (1981) Oxidation of substrates by isolated bacteroids and free-living cells of Rhizobium leguminosarum 3841. J Gen Microbiol 126:243–245
Hayaishi O, Katagiri M, Rothberg S (1957) Studies on oxygenases. Pyrocatechase. J Biol Chem 229:905–920
Kojima Y, Fujisawa H, Nakazawa A, Nakazawa T, Kanetsuna F, Toniuchi H, Nozaki M, Hayaishi O (1967) Studies on pyrocatechase. I. Purification and spectral properties. J Biol Chem 242:3270–3278
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 227:680–685
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurements with the Folin phenol reagent. J Biol Chem 193:265–275
Muthukumar G, Arunakumari A, Mahedevan A (1982) Degradation of aromatic compounds by Rhizobium spp. Plant and Soil 69:163–169
Nagami K, Senoh S (1974) Studies on the active site of Brevibacterium pyrocatechase. J Biochem 75:389–398
Nakagawa H, Inoue H, Takeda Y (1963) Characteristics of catechol oxygenase from Brevibacterium fuscum. J Biochem 54:65–74
Nakai C, Kagamiyama H, Saeki Y, Nozaki M (1979) Nonidentical subunits of pyrocatechase from Pseudomonas arvilla C-1. Arch Biochem Biophys 195:12–22
Nakazawa A, Kojima Y, Taniuchi H (1967) Purification and properties of pyrocatechase from Pseudomonas fluorescens. Biochim Biophys Acta 147:189–199
Nakazawa T, Nakazawa A (1970) Pyrocatechase (Pseudomonas). In: Tabor H, Tabor CW (eds) Methods in Enzymology, vol XVIIA. Academic Press, New York, pp 1–18
Ninnekar HZ, Vaidyanathan CS (1981) Catechol 1,2-dioxygenase from Aspergillus niger: purification and properties. J Indian Inst Sci 63:131–136
Ornstein L, Davis B (1962) Disc electrophoresis. Distillation Products Industries, Rochester, New York, USA
Parke D, Ornstein LN (1984) Nutritional diversity of Rhizobiaceae revealed by auxanography. J Gen Microbiol 130:1743–1750
Parker CA, Trinick MJ, Chatel DL (1977) Rhizobia as soil and rhizosphere inhabitants. In: A treatise on dinitrogen fixation, section IV. Agronomy and ecology. Wiley Publishing Company, New York, pp 311–352
Patel RN, Hou CT, Felix A, Lillard MO (1976) Catechol 1,2-dioxygenase from Acinetobacter calcoaceticus: purification and properties. J Bact 127:534–554
Saroso S, Glenn AR, Dilworth MJ (1984) Carbon utilization by free-living and bacteroid forms of cowpea Rhizobium NGR234. J Gen Microbiol 130:1809–1814
Stanier RY, Ornston LN (1973) The β-ketoadipate pathway. In: Rose AH, Tempest DW (eds) Advances in microbial physiology, vol 9. Academic Press, London New York, pp 89–149
Warburg O, Christian W (1939) Isolation and crystallization of proteins of the oxidative fermentation enzymes. Biochem Z 303:40–68
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Chen, Y.P., Glenn, A.R. & Dilworth, M.J. Aromatic metabolism in Rhizobium trifolii-catechol 1,2-dioxygenase. Arch. Microbiol. 141, 225–228 (1985). https://doi.org/10.1007/BF00408063
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00408063