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Identification of Bzd Subunits / Aromatoleum sp. CIB

ABSTRACT: Identification of enriched protein subunits after SDS-PAGE separation and tryptic digest by LC-MSE

INSTRUMENT(S): Synapt MS

ORGANISM(S): Azoarcus Sp. Cib Escherichia Coli

SUBMITTER: Jonathan Fuchs

LAB HEAD: Prof. Dr. Matthias Boll

PROVIDER: PXD053203 | Pride | 2025-05-07

REPOSITORIES: Pride

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			Action	DRS
	BzdN_20220610_LA_31.raw.zip	Raw
	BzdN_20220610_LA_31_IA_Log.txt	Txt
	BzdN_20220610_LA_31_IA_final_fragment.csv	Csv
	BzdN_20220610_LA_31_IA_final_peptide.csv	Csv
	BzdN_20220610_LA_31_IA_final_protein.csv	Csv

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Publications

Enzymatic Birch reduction via hydrogen atom transfer at [4Fe-4S]-OH<sub>2</sub> and [8Fe-9S] clusters.

Fuchs Jonathan J Fernández-Arévalo Unai U Demmer Ulrike U Díaz Eduardo E Ullmann G Matthias GM Pierik Antonio J AJ Ermler Ulrich U Boll Matthias M

Nature communications 20250404 1

The alkali metal- and ammonia-dependent Birch reduction is the classical synthetic method for achieving dihydro additions to arenes, typically yielding 1,4-cyclodienes. A mild biological alternative to this process are 1,5-dienoyl-coenzyme A (CoA)-forming class I and II benzoyl-CoA reductases (BCRs), widely abundant key enzymes in the biodegradation of aromatic compounds at anoxic environments. To obtain a comprehensive mechanistic understanding of class I BCR catalysis, we produced the active s ...[more]

PMID: 40185728

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