Details zur Publikation

Kategorie Textpublikation
Referenztyp Zeitschriften
DOI 10.1111/1462-2920.14784
Lizenz creative commons licence
Titel (primär) The class II benzoyl‐coenzyme A reductase complex from the sulfate‐reducing Desulfosarcina cetonica
Autor Anselmann, S.E.L.; Löffler, C.; Stärk, H.-J.; Jehmlich, N. ORCID logo ; von Bergen, M.; Brüls, T.; Boll, M.
Quelle Environmental Microbiology
Erscheinungsjahr 2019
Department ANA; MOLSYB
Band/Volume 21
Heft 11
Seite von 4241
Seite bis 4252
Sprache englisch
Supplements https://onlinelibrary.wiley.com/action/downloadSupplement?doi=10.1111%2F1462-2920.14784&file=emi14784-sup-0001-supinfo.docx
Abstract Benzoyl‐CoA reductases (BCRs) catalyse a key reaction in the anaerobic degradation pathways of monocyclic aromatic substrates, the dearomatization of benzoyl‐CoA (BzCoA) to cyclohexa‐1,5‐diene‐1‐carboxyl‐CoA (1,5‐dienoyl‐CoA) at the negative redox potential limit of diffusible enzymatic substrate/product couples (E°′ = −622 mV). A 1‐MDa class II BCR complex composed of the BamBCDEGHI subunits has so far only been isolated from the Fe(III)‐respiring Geobacter metallireducens. It is supposed to drive endergonic benzene ring reduction at an active site W‐pterin cofactor by flavin‐based electron bifurcation. Here, we identified multiple copies of putative genes encoding the structural components of a class II BCR in sulfate reducing, Fe(III)‐respiring and syntrophic bacteria. A soluble 950 kDa Bam[(BC)2DEFGHI]2 complex was isolated from extracts of Desulfosarcina cetonica cells grown with benzoate/sulfate. Metal and cofactor analyses together with the identification of conserved binding motifs gave rise to 4 W‐pterins, two selenocysteines, six flavin adenine dinucleotides, four Zn, and 48 FeS clusters. The complex exhibited 1,5‐dienoyl‐CoA‐, NADPH‐ and ferredoxin‐dependent oxidoreductase activities. Our results indicate that high‐molecular class II BCR metalloenzyme machineries are remarkably conserved in strictly anaerobic bacteria with regard to subunit architecture and cofactor content, but their subcellular localization and electron acceptor preference may differ as a result of adaptations to variable energy metabolisms.
dauerhafte UFZ-Verlinkung https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=22245
Anselmann, S.E.L., Löffler, C., Stärk, H.-J., Jehmlich, N., von Bergen, M., Brüls, T., Boll, M. (2019):
The class II benzoyl‐coenzyme A reductase complex from the sulfate‐reducing Desulfosarcina cetonica
Environ. Microbiol. 21 (11), 4241 - 4252 10.1111/1462-2920.14784