Biodegradation

, Volume 6, Issue 4, pp 295–308 | Cite as

A model for the effects of primary substrates on the kinetics of reductive dehalogenation

  • Brian A. Wrenn
  • Bruce E. Rittmann
Articles

Abstract

A kinetic model that describes substrate interactions during reductive dehalogenation reactions is developed. This model describes how the concentrations of primary electron-donor and -acceptor substrates affect the rates of reductive dehalogenation reactions. A basic model, which considers only exogenous electron-donor and -acceptor substrates, illustrates the fundamental interactions that affect reductive dehalogenation reaction kinetics. Because this basic model cannot accurately describe important phenomena, such as reductive dehalogenation that occurs in the absence of exogenous electron donors, it is expanded to include an endogenous electron donor and additional electron acceptor reactions. This general model more accurately reflects the behavior that has been observed for reductive dehalogenation reactions. Under most conditions, primary electron-donor substrates stimulate the reductive dehalogenation rate, while primary electron acceptors reduce the reaction rate. The effects of primary substrates are incorporated into the kinetic parameters for a Monod-like rate expression. The apparent maximum rate of reductive dehalogenation (q m, ap ) and the apparent half-saturation concentration (K ap ) increase as the electron donor concentration increases. The electron-acceptor concentration does not affect q m, ap , but K ap is directly proportional to its concentration.

Key words

reductive dehalogenation kinetics modeling substrate interactions cometabolism 

Definitions for model parameters

RX

halogenated aliphatic substrate

E-Mn

reduced dehalogenase

E-Mn+2

oxidized dehalogenase

[E-Mn]

steady-state concentration of the reduced dehalogenase (moles of reduced dehalogenase per unit volume)

[E-Mn+2]

steady-state concentration of the oxidized dehalogenase (moles of reduced dehalogenase per unit volume)

DH

primary exogenous electron-donor substrate

A

primary exogenous electron-acceptor substrate

A2

second primary exogenous electron-acceptor substrate

X

biomass concentration (biomass per unit volume)

f

fraction of biomass that is comprised of the dehalogenase (moles of dehalogenase per unit biomass)

α

stoichiometric coefficient for the reductive dehalogenation reaction (moles of dehalogenase oxidized per mole of halogenated substrate reduced)

β

stoichiometric coefficient for oxidation of the primary electron donor (moles of dehalogenase reduced per mole of donor oxidized)

γ

stoichiometric coefficient for oxidation of the endogenous electron donor (moles of dehalogenase reduced per unit biomass oxidized)

δ

stoichiometric coefficient for reduction of the primary electron acceptor (moles of dehalogenase oxidized per mole of acceptor reduced)

κ

stoichiometric coefficient for reduction of the second electron acceptor (moles of dehalogenase oxidized per mole of acceptor reduced)

rRX

rate of the reductive dehalogenation reaction (moles of halogenated substrate reduced per unit volume per unit time)

rd1

rate of oxidation of the primary exogenous electron donor (moles of donor oxidized per unit volume per unit time)

rd2

rate of oxidation of the endogenous electron donor (biomass oxidized per unit volume per unit time)

ra1

rate of reduction of the primary exogenous electron acceptor (moles of acceptor reduced per unit volume per unit time)

ra2

rate of reduction of the second primary electron acceptor (moles of acceptor reduced per unit volume per unit time)

kRX

mixed second-order rate coefficient for the reductive dehalogenation reaction (volume per mole dehalogenase per unit time)

kd1

mixed-second-order rate coefficient for oxidation of the primary electron donor (volume per mole dehalogenase per unit time)

kd2

mixed-second-order rate coefficient for oxidation of the endogenous electron donor (volume per mole dehalogenase per unit time)

b

first-order biomass decay coefficient (biomass oxidized per unit biomass per unit time)

ka1

mixed-second-order rate coefficient for reduction of the primary electron acceptor (volume per mole dehalogenase per unit time)

ka2

mixed-second-order rate coefficient for reduction of the second primary electron acceptor (volume per mole dehalogenase per unit time)

qm,ap

apparent maximum specific rate of reductive dehalogenation (moles of RX per unit biomass per unit time)

Kap

apparent half-saturation concentration for the halogenated aliphatic substrate (moles of RX per unit volume)

kap

apparent pseudo-first-order rate coefficient for reductive dehalogenation (volume per unit biomass per unit time)

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References

  1. Alvarez-Cohen L & McCarty PL (1991) Effects of toxicity, aeration, and reductant supply on trichloroethylene transformation by a mixed methanotrophic culture. Appl. Environ. Microbiol. 57: 228–235Google Scholar
  2. Costello DJ, Greenfield PF & Lee PL (1991) Dynamic modelling of a single-stage high-rate anaerobic reactor—II. Model verification. Water Res. 25: 859–871Google Scholar
  3. Criddle CS (1993) The kinetics of cometabolism. Biotech. Bioeng. 41: 1048–1056Google Scholar
  4. Criddle CS, DeWitt JT, Grbić-Galić D & McCarty PL (1990a) Transformation of carbon tetrachloride byPseudomonas sp. strain KC under denitrification conditions. Appl. Environ. Microbiol. 56: 3240–3246Google Scholar
  5. Criddle CS, DeWitt JT & McCarty PL (1990b) Reductive dehalogenation of carbon tetrachloride byE. coli K-12. Appl. Environ. Microbiol. 56: 3247–3254Google Scholar
  6. Dangel W, Schulz H, Diekert G, König H & Fuchs G (1987) Occurrence of corrinoid-containing membrane proteins in anaerobic bacteria. Arch. Microbiol. 148: 52–56Google Scholar
  7. DeWeerd KA & Suflita JM (1990) Anaerobic aryl reductive dehalogenation of halobenzoates by cell extracts ofDesulfomonile tiedjei. App. Environ. Microbiol. 56: 2999–3005Google Scholar
  8. DeWeerd KA, Concannon F & Suflita JM (1991) Relationship between hydrogen consumption, dehalogenation, and the reduction of sulfur oxyanions byDesulfomonile tiedjei. Appl. Environ. Microbiol. 57: 1929–1934Google Scholar
  9. Dolfing J & Tiedje JM (1991a) Acetate as a source of reducing equivalents in the reductive dechlorination of 2,5-dichlorobenzoate. Arch. Microbiol. 156: 356–361Google Scholar
  10. —— (1991b) Influence of substituents on reductive dehalogenation of 3-chlorobenzoate analogs. Appl. Environ. Microbiol. 57: 820–824Google Scholar
  11. Fathepure BZ & Boyd SA (1988) Dependence of tetrachloro-ethylene dechlorination on methanogenic substrate consumption byMethanosarcina sp. strain DCM. Appl. Environ. Microbiol. 54: 2976–2980Google Scholar
  12. Freedman DL & Gossett JM (1989) Biological reductive dechlorination of tetrachloroethylene and trichloroethylene to ethylene under methanogenic conditions. Appl. Environ. Microbiol. 55: 2144–2151Google Scholar
  13. Gälli R & McCarty PL (1989) Kinetics of biotransformation of 1,1,1-trichloroethane byClostridium sp. strain TCAIIB. Appl. Environ. Microbiol. 55: 845–851Google Scholar
  14. Gantzer CJ & Wackett LP (1991) Reductive dechlorination catalyzed by bacterial transition-metal coenzymes. Environ. Sci. Tech. 25: 715–722Google Scholar
  15. Gibson SA & Suflita JM (1990) Anaerobic biodegradation of 2,4,5-trichlorophenoxyacetic acid in samples from a methanogenic aquifer: Stimulation by short-chain organic acids and alcohols. Appl. Environ. Microbiol. 56: 1825–1832Google Scholar
  16. —— (1993) Role of electron-donating cosubstrates in the anaerobic biotransformation of chlorophenoxyacetates to chlorophenols by a bacterial consortium enriched on phenoxyacetate. Biodegradation 4: 51–57Google Scholar
  17. Gottschalk G (1986) Bacterial Metabolism, Second Edition. Springer-Verlag, New YorkGoogle Scholar
  18. Henry SM & Grbić-Galić D (1991) Influence of endogenous and exogenous electron donors and trichloroethylene oxidation toxicity on trichloroethylene oxidation by methanotrophic cultures from a groundwater aquifer. Appl. Environ. Microbiol. 57: 236–244Google Scholar
  19. Ingvorsen K & Jorgensen BB (1984) Kinetics of sulfate uptake by freshwater and marine species ofDesulfovibrio. Arch. Microbiol. 139: 61–66Google Scholar
  20. Ingvorsen K, Zehnder AJB & Jorgensen BB (1984) Kinetics of sulfate and acetate uptake byDesulfobacter postgatei. Appl. Environ. Microbiol. 47: 403–408Google Scholar
  21. Jones WJ, Nagle DP Jr & Whitman WB (1987) Methanogens and the diversity of archaebacteria. Microbiological Reviews 51: 135–177Google Scholar
  22. Klecka GM & Gonsior SJ (1984) Reductive dechlorination of chlorinated methanes and ethanes by reduced iron (II) porphyrins. Chemosphere 13: 391–402Google Scholar
  23. Kochi JK (1978) Organometallic Mechanisms and Catalysis. Academic Press, New YorkGoogle Scholar
  24. Krone UE, Thauer RK & Hogenkamp HPC (1989a) Reductive dehalogenation of chlorinated C1-hydrocarbons mediated by corrinoids. Biochemistry 28: 4908–4914Google Scholar
  25. Krone UE, Laufer K, Thauer RK & Hogenkamp HPC (1989b) Coenzyme F430 as a possible catalyst for the reductive dehalogenation of chlorinated C1 hydrocarbons in methanogenic bacteria. Biochemistry 28: 10,061–10,065Google Scholar
  26. Kuhn EP, Townsend GT & Suflita JM (1990) Effect of sulfate and organic carbon supplements on reductive dehalogenation of chloroanilines in anaerobic aquifer slurries. Appl. Environ. Microbiol. 56: 2630–2637Google Scholar
  27. McCarty PL (1972) Energetics of organic matter degradation. In: Mitchell R (Ed) Water Pollution Microbiology. (pp 91–118) Wiley-Interscience, New YorkGoogle Scholar
  28. Mikesell MD & Boyd SA (1990) Dechlorination of chloroform byMethanosarcina strains. Appl. Environ. Microbiol. 56: 1198–1201Google Scholar
  29. Nethe-Jaenchen R & Thauer RK (1984) Growth yields and saturation constant ofDesulfovibrio vulgaris in chemostat culture. Arch. Microbiol. 137: 236–240Google Scholar
  30. Saéz PB & Rittmann BE (1993) Biodegradation kinetics of a mixture containing a primary substrate (phenol) and an inhibitory cometabolite (4-chlorophenol). Biodegradation 4: 3–21Google Scholar
  31. Schauer NL, Brown DP & Ferry JG (1982) Kinetics of formate metabolism inMethanobacterium formicicum andMethanospirillum hungatei. Appl. Environ. Microbiol. 44: 549–554Google Scholar
  32. Wade RS & Castro CE (1973a) Oxidation of iron (II) porphyrins by alkyl halides. J. Amer. Chem. Soc. 95: 226–230Google Scholar
  33. —— (1973b) Oxidation of heme proteins by alkyl halides. J. Amer. Chem. Soc. 95: 231–234Google Scholar
  34. Widdel F (1988) Microbiology and ecology of sulfate- and sulfur-reducing bacteria. In: Zehnder AJB (Ed) Biology of Anaerobic Microorganisms. (pp 468–585) John Wiley and Sons, Inc., New YorkGoogle Scholar
  35. Wrenn BA & Rittmann BE Experimental evaluation of a model for the effects of primary substrates on reductive dehalogenation kinetics. Submitted to BiodegradationGoogle Scholar
  36. Zeikus JG, Kerby R & Krzycki JA (1985) Single-carbon chemistry of acetogenic and methanogenic bacteria. Science 227: 1167–1173Google Scholar

Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Brian A. Wrenn
    • 1
  • Bruce E. Rittmann
    • 2
  1. 1.Department of Civil and Environmental EngineeringUniversity of CincinnatiCincinnatiUSA
  2. 2.Department of Civil EngineeringNorthwestern UniversityEvanstonUSA

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