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Reference Category Journals
DOI 10.1111/1462-2920.14784
Licence creative commons licence
Title (Primary) The class II benzoyl‐coenzyme A reductase complex from the sulfate‐reducing Desulfosarcina cetonica
Author Anselmann, S.E.L.; Löffler, C.; Stärk, H.-J.; Jehmlich, N. ORCID logo ; von Bergen, M.; Brüls, T.; Boll, M.
Source Titel Environmental Microbiology
Year 2019
Department ANA; MOLSYB
Volume 21
Issue 11
Page From 4241
Page To 4252
Language 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.
Persistent UFZ Identifier 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