<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Sedlacek V</submitter><funding>Czech Science Foundation</funding><funding>Grant Agency of Masaryk University</funding><pagination>902</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9137774</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(5)</volume><pubmed_abstract>&lt;i>Paracoccus denitrificans&lt;/i> ArsH is encoded by two identical genes located in two distinct putative arsenic resistance (&lt;i>ars&lt;/i>) operons. &lt;i>Escherichia coli&lt;/i>-produced recombinant N-His&lt;sub>6&lt;/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&lt;sub>2&lt;/sub>) and formation of phenylarsonous acid were observed.</pubmed_abstract><journal>Antioxidants (Basel, Switzerland)</journal><pubmed_title>The ArsH Protein Product of the &lt;i>Paracoccus denitrificans ars&lt;/i> Operon Has an Activity of Organoarsenic Reductase and Is Regulated by a Redox-Responsive Repressor.</pubmed_title><pmcid>PMC9137774</pmcid><funding_grant_id>GA 16-18476S</funding_grant_id><funding_grant_id>MUNI/A/1604/2020</funding_grant_id><pubmed_authors>Kucera I</pubmed_authors><pubmed_authors>Sedlacek V</pubmed_authors><pubmed_authors>Kryl M</pubmed_authors></additional><is_claimable>false</is_claimable><name>The ArsH Protein Product of the &lt;i>Paracoccus denitrificans ars&lt;/i> Operon Has an Activity of Organoarsenic Reductase and Is Regulated by a Redox-Responsive Repressor.</name><description>&lt;i>Paracoccus denitrificans&lt;/i> ArsH is encoded by two identical genes located in two distinct putative arsenic resistance (&lt;i>ars&lt;/i>) operons. &lt;i>Escherichia coli&lt;/i>-produced recombinant N-His&lt;sub>6&lt;/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&lt;sub>2&lt;/sub>) and formation of phenylarsonous acid were observed.</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 May</publication><modification>2026-04-08T10:24:43.84Z</modification><creation>2024-11-15T11:14:39.142Z</creation></dates><accession>S-EPMC9137774</accession><cross_references><pubmed>35624766</pubmed><doi>10.3390/antiox11050902</doi></cross_references></HashMap>