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http://purl.uniprot.org/citations/11602591http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11602591http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11602591http://www.w3.org/2000/01/rdf-schema#comment"4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a key enzyme in the anaerobic metabolism of phenolic compounds. It catalyzes the reductive removal of the hydroxyl group from the aromatic ring yielding benzoyl-CoA and water. The subunit architecture, amino acid sequence, and the cofactor/metal content indicate that it belongs to the xanthine oxidase (XO) family of molybdenum cofactor-containing enzymes. 4-HBCR is an unusual XO family member as it catalyzes the irreversible reduction of a CoA-thioester substrate. A radical mechanism has been proposed for the enzymatic removal of phenolic hydroxyl groups. In this work we studied the spectroscopic and electrochemical properties of 4-HBCR by EPR and Mössbauer spectroscopy and identified the pterin cofactor as molybdopterin mononucleotide. In addition to two different [2Fe-2S] clusters, one FAD and one molybdenum species per monomer, we also identified a [4Fe-4S] cluster/monomer, which is unique among members of the XO family. The reduced [4Fe-4S] cluster interacted magnetically with the Mo(V) species, suggesting that the centers are in close proximity, (<15 A apart). Additionally, reduction of the [4Fe-4S] cluster resulted in a loss of the EPR signals of the [2Fe-2S] clusters probably because of magnetic interactions between the Fe-S clusters as evidenced in power saturation studies. The Mo(V) EPR signals of 4-HBCR were typical for XO family members. Under steady-state conditions of substrate reduction, in the presence of excess dithionite, the [4Fe-4S] clusters were in the fully oxidized state while the [2Fe-2S] clusters remained reduced. The redox potentials of the redox cofactors were determined to be: [2Fe-2S](+1/+2) I, -205 mV; [2Fe-2S] (+1/+2) II, -255 mV; FAD/FADH( small middle dot)/FADH, -250 mV/-470 mV; [4Fe-4S](+1/+2), -465 mV and Mo(VI)/(V)/(VI), -380 mV/-500 mV. A catalytic cycle is proposed that takes into account the common properties of molybdenum cofactor enzymes and the special one-electron chemistry of dehydroxylation of phenolic compounds."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m106766200"xsd:string
http://purl.uniprot.org/citations/11602591http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m106766200"xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Boll M."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Boll M."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Fuchs G."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Fuchs G."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Ragsdale S.W."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Ragsdale S.W."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Meier C."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Meier C."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Lowe D.J."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Lowe D.J."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Buchanan G."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Buchanan G."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"El Kasmi A."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"El Kasmi A."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Trautwein A."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/author"Trautwein A."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11602591http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
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