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A catalytically versatile benzoyl-CoA reductase, key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria.

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Title: A catalytically versatile benzoyl-CoA reductase, key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria.
Authors: Tiedt, Oliver1, Fuchs, Jonathan1, Eisenreich, Wolfgang2, Boll, Matthias1 matthias.boll@biologie.uni-freiburg.de
Source: Journal of Biological Chemistry. 6/29/2018, Vol. 293 Issue 26, p10264-10274. 11p. 3 Diagrams, 2 Charts, 4 Graphs.
Subjects: Coenzyme A, Reductases, Catalytic activity, Biodegradation, Denitrifying bacteria, Aromatic compound analysis, Benzoates
Abstract: Class I benzoyl-CoA (BzCoA) reductases (BCRs) are key enzymes in the anaerobic degradation of aromatic compounds. They catalyze the ATP-dependent reduction of the central BzCoA intermediate and analogues of it to conjugated cyclic 1,5-dienoyl-CoAs probably by a radical-based, Birch-like reduction mechanism. Discovered in 1995, the enzyme from the denitrifying bacterium Thauera aromatica (BCRTar) has so far remained the only isolated and biochemically accessible BCR, mainly because BCRs are extremely labile, and their heterologous production has largely failed so far. Here, we describe a platform for the heterologous expression of the four structural genes encoding a designated 3-methylbenzoyl-CoA reductase from the related denitrifying species Thauera chlorobenzoica (MBRTcl) in Escherichia coli. This reductase represents the prototype of a distinct subclass of ATP-dependent BCRs that were proposed to be involved in the degradation of methyl-substituted BzCoA analogues. The recombinant MBRTcl had an αβγδ-subunit architecture, contained three low-potential [4Fe-4S] clusters, and was highly oxygen-labile. It catalyzed the ATP-dependent reductive dearomatization of BzCoA with 2.3–2.8 ATPs hydrolyzed per two electrons transferred and preferentially dearomatized methyl- and chloro-substituted analogues in meta- and para-positions. NMR analyses revealed that 3-methylbenzoyl-CoA is regioselectively reduced to 3-methyl-1,5-dienoyl-CoA. The unprecedented reductive dechlorination of 4-chloro-BzCoA to BzCoA probably via HCl elimination from a reduced intermediate allowed for the previously unreported growth of T. chlorobenzoica on 4-chlorobenzoate. The heterologous expression platform established in this work enables the production, isolation, and characterization of bacterial and archaeal BCR and BCR-like radical enzymes, for many of which the function has remained unknown. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: A catalytically versatile benzoyl-CoA reductase, key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria.
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  Data: <searchLink fieldCode="AR" term="%22Tiedt%2C+Oliver%22">Tiedt, Oliver</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Fuchs%2C+Jonathan%22">Fuchs, Jonathan</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Eisenreich%2C+Wolfgang%22">Eisenreich, Wolfgang</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Boll%2C+Matthias%22">Boll, Matthias</searchLink><relatesTo>1</relatesTo><i> matthias.boll@biologie.uni-freiburg.de</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 6/29/2018, Vol. 293 Issue 26, p10264-10274. 11p. 3 Diagrams, 2 Charts, 4 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Coenzyme+A%22">Coenzyme A</searchLink><br /><searchLink fieldCode="DE" term="%22Reductases%22">Reductases</searchLink><br /><searchLink fieldCode="DE" term="%22Catalytic+activity%22">Catalytic activity</searchLink><br /><searchLink fieldCode="DE" term="%22Biodegradation%22">Biodegradation</searchLink><br /><searchLink fieldCode="DE" term="%22Denitrifying+bacteria%22">Denitrifying bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Aromatic+compound+analysis%22">Aromatic compound analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Benzoates%22">Benzoates</searchLink>
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  Data: Class I benzoyl-CoA (BzCoA) reductases (BCRs) are key enzymes in the anaerobic degradation of aromatic compounds. They catalyze the ATP-dependent reduction of the central BzCoA intermediate and analogues of it to conjugated cyclic 1,5-dienoyl-CoAs probably by a radical-based, Birch-like reduction mechanism. Discovered in 1995, the enzyme from the denitrifying bacterium Thauera aromatica (BCRTar) has so far remained the only isolated and biochemically accessible BCR, mainly because BCRs are extremely labile, and their heterologous production has largely failed so far. Here, we describe a platform for the heterologous expression of the four structural genes encoding a designated 3-methylbenzoyl-CoA reductase from the related denitrifying species Thauera chlorobenzoica (MBRTcl) in Escherichia coli. This reductase represents the prototype of a distinct subclass of ATP-dependent BCRs that were proposed to be involved in the degradation of methyl-substituted BzCoA analogues. The recombinant MBRTcl had an αβγδ-subunit architecture, contained three low-potential [4Fe-4S] clusters, and was highly oxygen-labile. It catalyzed the ATP-dependent reductive dearomatization of BzCoA with 2.3–2.8 ATPs hydrolyzed per two electrons transferred and preferentially dearomatized methyl- and chloro-substituted analogues in meta- and para-positions. NMR analyses revealed that 3-methylbenzoyl-CoA is regioselectively reduced to 3-methyl-1,5-dienoyl-CoA. The unprecedented reductive dechlorination of 4-chloro-BzCoA to BzCoA probably via HCl elimination from a reduced intermediate allowed for the previously unreported growth of T. chlorobenzoica on 4-chlorobenzoate. The heterologous expression platform established in this work enables the production, isolation, and characterization of bacterial and archaeal BCR and BCR-like radical enzymes, for many of which the function has remained unknown. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1074/jbc.RA118.003329
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      – Code: eng
        Text: English
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        PageCount: 11
        StartPage: 10264
    Subjects:
      – SubjectFull: Coenzyme A
        Type: general
      – SubjectFull: Reductases
        Type: general
      – SubjectFull: Catalytic activity
        Type: general
      – SubjectFull: Biodegradation
        Type: general
      – SubjectFull: Denitrifying bacteria
        Type: general
      – SubjectFull: Aromatic compound analysis
        Type: general
      – SubjectFull: Benzoates
        Type: general
    Titles:
      – TitleFull: A catalytically versatile benzoyl-CoA reductase, key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria.
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            NameFull: Tiedt, Oliver
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            NameFull: Fuchs, Jonathan
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            NameFull: Eisenreich, Wolfgang
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              Text: 6/29/2018
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              Y: 2018
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