Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase

Boll, Matthias; Einsle, Oliver; Ermler, Ulrich; Kroneck, Peter M. H.; Ullmann, G. Matthias

Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase

Dateien

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Datum

2016

Autor:innen

Boll, Matthias

Einsle, Oliver

Ermler, Ulrich

Kroneck, Peter M. H.

Ullmann, G. Matthias

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Journal of Molecular Microbiology and Biotechnology. 2016, 26(1-3), pp. 119-137. ISSN 1464-1801. eISSN 1660-2412. Available under: doi: 10.1159/000440805

Zusammenfassung

In biology, tungsten (W) is exclusively found in microbial enzymes bound to a bis-pyranopterin cofactor (bis-WPT). Previously known W enzymes catalyze redox oxo/hydroxyl transfer reactions by directly coordinating their substrates or products to the metal. They comprise the W-containing formate/formylmethanofuran dehydrogenases belonging to the dimethyl sulfoxide reductase (DMSOR) family and the aldehyde:ferredoxin oxidoreductase (AOR) families, which form a separate enzyme family within the Mo/W enzymes. In the last decade, initial insights into the structure and function of two unprecedented W enzymes were obtained: the acetaldehyde forming acetylene hydratase (ACH) belongs to the DMSOR and the class II benzoyl-coenzyme A (CoA) reductase (BCR) to the AOR family. The latter catalyzes the reductive dearomatization of benzoyl-CoA to a cyclic diene. Both are key enzymes in the degradation of acetylene (ACH) or aromatic compounds (BCR) in strictly anaerobic bacteria. They are unusual in either catalyzing a nonredox reaction (ACH) or a redox reaction without coordinating the substrate or product to the metal (BCR). In organic chemical synthesis, analogous reactions require totally nonphysiological conditions depending on Hg2+ (acetylene hydration) or alkali metals (benzene ring reduction). The structural insights obtained pave the way for biological or biomimetic approaches to basic reactions in organic chemistry.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

BOLL, Matthias, Oliver EINSLE, Ulrich ERMLER, Peter M. H. KRONECK, G. Matthias ULLMANN, 2016. Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase. In: Journal of Molecular Microbiology and Biotechnology. 2016, 26(1-3), pp. 119-137. ISSN 1464-1801. eISSN 1660-2412. Available under: doi: 10.1159/000440805

BibTex

@article{Boll2016-03-10Struc-33648,
  year={2016},
  doi={10.1159/000440805},
  title={Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase},
  number={1-3},
  volume={26},
  issn={1464-1801},
  journal={Journal of Molecular Microbiology and Biotechnology},
  pages={119--137},
  author={Boll, Matthias and Einsle, Oliver and Ermler, Ulrich and Kroneck, Peter M. H. and Ullmann, G. Matthias}
}

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