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MetaCyc Pathway: chlorate reduction

Enzyme View:

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Generation of Precursor Metabolites and Energy Respiration Anaerobic Respiration

Some taxa known to possess this pathway include ? : Alicycliphilus denitrificans , Azospira oryzae , Dechloromonas aromatica , Ideonella dechloratans , Pseudomonas chloritidismutans , Sulfolobus islandicus

Expected Taxonomic Range: Archaea , Bacteria

Summary:
General Background

Like fermentation, respiration is a process by which electrons are passed from an electron donor to a terminal electron acceptor. However, in respiration the electrons do not pass directly from the donor to the acceptor. Instead, they pass a number of membrane-bound electron carriers that function as a transport chain, passing the electrons from one to another in steps that follow the electrochemical gradients between the electron donor and the acceptor.

Each oxidized member of the electron transfer chain (which can be a flavoprotein, an electron-transfer-related quinone, a cytochrome, or other type of electron carrier) can be reduced by the reduced form of the preceding member, and the electrons flow through the chain all the way to the terminal acceptor, which could be oxygen in the case of aerobic respiration, or another type of molecule in anaerobic respiration.

Known terminal acceptors include organic compounds (fumarate, dimethyl sulfoxide, or trimethylamine N-oxide), or inorganic compounds (nitrate, nitrite, nitrous oxide, chlorate, perchlorate, oxidized manganese ions, ferric iron, gold, selenate, arsenate, sulfate and elemental sulfur).

During the process of electron transfer, a proton gradient is formed across the membrane due to three potential processes:

1. The use of some of the energy associated with the electron transfer for active pumping of protons out of the cell.

2. Exporting protons out of the cell during electron-to-hydrogen transfers.

3. Scalar reactions that consume protons inside the cell, or produce them outside the cell, without actually moving a proton from one compartment to another.

Upon passage of protons back into the cytoplasm, they drive multisubunit ATP synthase enzymes that generate ATP.

About This Pathway

(Per)chlorate-reducing bacteria use the highly oxidized chlorate ion as the sole electron acceptor for oxidation of organic matter. The reduction of chlorate occurs in a two-step reaction: chlorate reduction to chlorite, followed by the decomposition of the latter to chloride ions and oxygen. The second step is one of the rare occasions where molecular oxygen is formed in a metabolic reaction [other examples include photosynthesis, the detoxification of reactive oxygen species (see for example superoxide radicals degradation), and potentially the reaction catalyzed by "nitric oxide lyase" (see intra-aerobic nitrite reduction)].

The two enzymes that catalyze chlorate reduction, chlorate reductase and chlorite dismutase, are periplasmic, and have been purified from several organisms [Thorell03, deGeus09]. Electron transport from the bacterial inner membrane to the soluble periplasmic chlorate reductase is mediated by soluble c cytochromes [Bohlin09], while additional c cytochromes present in the periplasm appear to serve as electron donors for the terminal oxidase [Backlund09].

The oxygen that is produced in the process is believed to be used by either terminal oxidases or by monooxygenases that attack hydrocarbons, enabling the organisms to use oxygen-requiring enzymes under anaerobic conditions [Chakraborty04a].

Credits:
Created 14-Jun-2010 by Caspi R , SRI International


References

Backlund09: Backlund AS, Bohlin J, Gustavsson N, Nilsson T (2009). "Periplasmic c cytochromes and chlorate reduction in Ideonella dechloratans." Appl Environ Microbiol 75(8);2439-45. PMID: 19233956

Bohlin09: Bohlin J, Backlund AS, Gustavsson N, Wahlberg S, Nilsson T (2009). "Characterization of a cytochrome c gene located at the gene cluster for chlorate respiration in Ideonella dechloratans." Microbiol Res. PMID: 20015627

Chakraborty04a: Chakraborty R, Coates JD (2004). "Anaerobic degradation of monoaromatic hydrocarbons." Appl Microbiol Biotechnol 64(4);437-46. PMID: 14735323

deGeus09: de Geus DC, Thomassen EA, Hagedoorn PL, Pannu NS, van Duijn E, Abrahams JP (2009). "Crystal structure of chlorite dismutase, a detoxifying enzyme producing molecular oxygen." J Mol Biol 387(1);192-206. PMID: 19361444

Franz07: Franz B, Lichtenberg H, Hormes J, Modrow H, Dahl C, Prange A (2007). "Utilization of solid "elemental" sulfur by the phototrophic purple sulfur bacterium Allochromatium vinosum: a sulfur K-edge X-ray absorption spectroscopy study." Microbiology 153(Pt 4);1268-74. PMID: 17379736

Malmqvist91: Malmqvist A, Welander T, Gunnarsson L (1991). "Anaerobic Growth of Microorganisms with Chlorate as an Electron Acceptor." Appl Environ Microbiol 57(8);2229-2232. PMID: 16348537

Steudel00: Steudel, R. (2000). "The chemical sulfur cycle." Environmental Technologies to Treat Sulfur Pollution, pp. 1-31. Edited by P. N. L. Lens & L. Hulshof Pol. London: IWA Publishing.

Thorell03: Thorell HD, Stenklo K, Karlsson J, Nilsson T (2003). "A gene cluster for chlorate metabolism in Ideonella dechloratans." Appl Environ Microbiol 69(9);5585-92. PMID: 12957948

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Mehboob09: Mehboob F, Wolterink AF, Vermeulen AJ, Jiang B, Hagedoorn PL, Stams AJ, Kengen SW (2009). "Purification and characterization of a chlorite dismutase from Pseudomonas chloritidismutans." FEMS Microbiol Lett 293(1);115-21. PMID: 19228194

OConnor02: O'Connor SM, Coates JD (2002). "Universal immunoprobe for (per)chlorate-reducing bacteria." Appl Environ Microbiol 68(6);3108-13. PMID: 12039773


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, biocyc13.