Initial characterization of a reductive dehalogenase from Desulfitobacterium chlororespirans Co23

Desulfitobacterium chlororespirans Co23 is capable of using 3-chloro-4-hydroxybenzoate as terminal electron acceptor for growth. Membrane preparations from cells grown fermentatively on pyruvate in the presence of 3-chloro-4-hydroxybenzoate dechlorinated this compound at a rate of 3.9 nmol min-1 mg...

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Veröffentlicht in:Applied and Environmental Microbiology 1996-10, Vol.62 (10), p.3809-3813
Hauptverfasser: Loffler, F.E. (Michigan State University, East Lansing, MI.), Sanford, R.A, Tiedje, J.M
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creator Loffler, F.E. (Michigan State University, East Lansing, MI.)
Sanford, R.A
Tiedje, J.M
description Desulfitobacterium chlororespirans Co23 is capable of using 3-chloro-4-hydroxybenzoate as terminal electron acceptor for growth. Membrane preparations from cells grown fermentatively on pyruvate in the presence of 3-chloro-4-hydroxybenzoate dechlorinated this compound at a rate of 3.9 nmol min-1 mg of protein-1. Fivefold-greater dechlorination rates were measured with reduced methyl viologen as the artificial electron donor. Reduced benzyl viologen, NADH, NADPH, reduced flavin adenine dinucleotide, and reduced flavin mononucleotide could not substitute for reduced methyl viologen. The maximal initial rate of catalysis was achieved at pH 6.5 and 60 degrees C. The membrane-bound dechlorinating enzyme system was not oxygen sensitive and was stable at 57 degrees C for at least 2 h. Sulfite inhibited dechlorination in cell-free assays, whereas sulfate did not. Several chlorophenols were dehalogenated exclusively in the ortho position by cell extracts
doi_str_mv 10.1128/aem.62.10.3809-3813.1996
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(Michigan State University, East Lansing, MI.) ; Sanford, R.A ; Tiedje, J.M</creator><creatorcontrib>Loffler, F.E. (Michigan State University, East Lansing, MI.) ; Sanford, R.A ; Tiedje, J.M</creatorcontrib><description>Desulfitobacterium chlororespirans Co23 is capable of using 3-chloro-4-hydroxybenzoate as terminal electron acceptor for growth. Membrane preparations from cells grown fermentatively on pyruvate in the presence of 3-chloro-4-hydroxybenzoate dechlorinated this compound at a rate of 3.9 nmol min-1 mg of protein-1. Fivefold-greater dechlorination rates were measured with reduced methyl viologen as the artificial electron donor. Reduced benzyl viologen, NADH, NADPH, reduced flavin adenine dinucleotide, and reduced flavin mononucleotide could not substitute for reduced methyl viologen. The maximal initial rate of catalysis was achieved at pH 6.5 and 60 degrees C. The membrane-bound dechlorinating enzyme system was not oxygen sensitive and was stable at 57 degrees C for at least 2 h. Sulfite inhibited dechlorination in cell-free assays, whereas sulfate did not. 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(Michigan State University, East Lansing, MI.)</creatorcontrib><creatorcontrib>Sanford, R.A</creatorcontrib><creatorcontrib>Tiedje, J.M</creatorcontrib><title>Initial characterization of a reductive dehalogenase from Desulfitobacterium chlororespirans Co23</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>Desulfitobacterium chlororespirans Co23 is capable of using 3-chloro-4-hydroxybenzoate as terminal electron acceptor for growth. Membrane preparations from cells grown fermentatively on pyruvate in the presence of 3-chloro-4-hydroxybenzoate dechlorinated this compound at a rate of 3.9 nmol min-1 mg of protein-1. Fivefold-greater dechlorination rates were measured with reduced methyl viologen as the artificial electron donor. Reduced benzyl viologen, NADH, NADPH, reduced flavin adenine dinucleotide, and reduced flavin mononucleotide could not substitute for reduced methyl viologen. 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(Michigan State University, East Lansing, MI.)</au><au>Sanford, R.A</au><au>Tiedje, J.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Initial characterization of a reductive dehalogenase from Desulfitobacterium chlororespirans Co23</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>1996-10-01</date><risdate>1996</risdate><volume>62</volume><issue>10</issue><spage>3809</spage><epage>3813</epage><pages>3809-3813</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><abstract>Desulfitobacterium chlororespirans Co23 is capable of using 3-chloro-4-hydroxybenzoate as terminal electron acceptor for growth. Membrane preparations from cells grown fermentatively on pyruvate in the presence of 3-chloro-4-hydroxybenzoate dechlorinated this compound at a rate of 3.9 nmol min-1 mg of protein-1. Fivefold-greater dechlorination rates were measured with reduced methyl viologen as the artificial electron donor. Reduced benzyl viologen, NADH, NADPH, reduced flavin adenine dinucleotide, and reduced flavin mononucleotide could not substitute for reduced methyl viologen. The maximal initial rate of catalysis was achieved at pH 6.5 and 60 degrees C. The membrane-bound dechlorinating enzyme system was not oxygen sensitive and was stable at 57 degrees C for at least 2 h. Sulfite inhibited dechlorination in cell-free assays, whereas sulfate did not. Several chlorophenols were dehalogenated exclusively in the ortho position by cell extracts</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>16535425</pmid><doi>10.1128/aem.62.10.3809-3813.1996</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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source ASM_美国微生物学会期刊; PubMed Central; Alma/SFX Local Collection
subjects ACIDE BENZOIQUE
ACIDO BENZOICO
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
ANAEROBIOSE
ANAEROBIOSIS
BACTERIA
BACTERIA GRAM POSITIVA
BACTERIE GRAM POSITIF
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
CHLORE
CLORO
COMPOSE ORGANOCHLORE
COMPUESTO ORGANICO DEL CLORO
Desulfitobacterium chlororespirans
Enzymes
FLORA DEL SUELO
FLORE DU SOL
Fundamental and applied biological sciences. Psychology
Microbiology
MICROORGANISME
MICROORGANISMOS
Microorganisms
Mission oriented research
Oxidation
OXIDORREDUCTASAS
OXIGENO
OXIRREDUCION
OXYDOREDUCTASE
OXYDOREDUCTION
OXYGENE
Physiology and metabolism
REACCIONES QUIMICAS
REACTION CHIMIQUE
REDUCCION
REDUCTION
TEMPERATURA
TEMPERATURE
title Initial characterization of a reductive dehalogenase from Desulfitobacterium chlororespirans Co23
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