Abstract
AbstractThe dehydroxylating 4‐hydroxybenzoyl‐CoA reductase (HBCR) plays an important role in the degradation ofpara‐hydroxylated aromatic compounds in anaerobic bacteria. The enzyme catalyzes the removal of the phenolic hydroxyl group from 4‐hydroxybenzoyl‐CoA, yielding benzoyl‐CoA and water; a reduced ferredoxin serves as an electron donor. The enzyme belongs to the xanthine oxidase (XO) family of molybdenum cofactor containing enzymes and contains a molybdopterin‐cytosine dinucleotide cofactor, two [2Fe–2S] clusters, FAD and a [4Fe–4S] cluster per functional unit. HBCR is unique among XO family members in catalyzing the irreversible reduction of the substrate. A mechanism that differs from all other XO membersviahighly reactive radical intermediates has been suggested. The structural, electrochemical, spectroscopic, and kinetic properties of HBCR fromThauera aromaticaare highlighted and compared with other members of the xanthine oxidase family.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
