{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sedlacek V"],"funding":["Czech Science Foundation","Grant Agency of Masaryk University"],"pagination":["902"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9137774"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(5)"],"pubmed_abstract":["<i>Paracoccus denitrificans</i> ArsH is encoded by two identical genes located in two distinct putative arsenic resistance (<i>ars</i>) operons. <i>Escherichia coli</i>-produced recombinant N-His<sub>6</sub>-ArsH was characterized both structurally and kinetically. The X-ray structure of ArsH revealed a flavodoxin-like domain and motifs for the binding of flavin mononucleotide (FMN) and reduced nicotinamide adenine dinucleotide phosphate (NADPH). The protein catalyzed FMN reduction by NADPH via ternary complex mechanism. At a fixed saturating FMN concentration, it acted as an NADPH-dependent organoarsenic reductase displaying ping-pong kinetics. A 1:1 enzymatic reaction of phenylarsonic acid with the reduced form of FMN (FMNH<sub>2</sub>) and formation of phenylarsonous acid were observed."],"journal":["Antioxidants (Basel, Switzerland)"],"pubmed_title":["The ArsH Protein Product of the <i>Paracoccus denitrificans ars</i> Operon Has an Activity of Organoarsenic Reductase and Is Regulated by a Redox-Responsive Repressor."],"pmcid":["PMC9137774"],"funding_grant_id":["GA 16-18476S","MUNI/A/1604/2020"],"pubmed_authors":["Kucera I","Sedlacek V","Kryl M"],"additional_accession":[]},"is_claimable":false,"name":"The ArsH Protein Product of the <i>Paracoccus denitrificans ars</i> Operon Has an Activity of Organoarsenic Reductase and Is Regulated by a Redox-Responsive Repressor.","description":"<i>Paracoccus denitrificans</i> ArsH is encoded by two identical genes located in two distinct putative arsenic resistance (<i>ars</i>) operons. <i>Escherichia coli</i>-produced recombinant N-His<sub>6</sub>-ArsH was characterized both structurally and kinetically. The X-ray structure of ArsH revealed a flavodoxin-like domain and motifs for the binding of flavin mononucleotide (FMN) and reduced nicotinamide adenine dinucleotide phosphate (NADPH). The protein catalyzed FMN reduction by NADPH via ternary complex mechanism. At a fixed saturating FMN concentration, it acted as an NADPH-dependent organoarsenic reductase displaying ping-pong kinetics. A 1:1 enzymatic reaction of phenylarsonic acid with the reduced form of FMN (FMNH<sub>2</sub>) and formation of phenylarsonous acid were observed.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2026-04-08T10:24:43.84Z","creation":"2024-11-15T11:14:39.142Z"},"accession":"S-EPMC9137774","cross_references":{"pubmed":["35624766"],"doi":["10.3390/antiox11050902"]}}