ArticleThe Journal of biological chemistry2016
Perchlorate Reductase Is Distinguished by Active Site Aromatic Gate Residues.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Advances in the DMSO reductase family: From discovery to mechanism.Current opinion in chemical biology · 2026Review
- Catalytic Reduction of Aqueous Perchlorate at Neutral pH.ACS central science · 2026Article
- Structure and function of periplasmic nitrate reductase.Biochemical Society transactions · 2026Review
- Donor-acceptor catalysis with defective MoSNature communications · 2026Article
- A di-nuclear μ-oxido rhenium(VI) complex: from deep purple to catalytic applications.Dalton transactions (Cambridge, England : 2003) · 2026Article
- Investigating the role of bacterial raw milk community members in chlorate reduction.Access microbiology · 2026Article
- Genetic identification of the selenate reductase inApplied and environmental microbiology · 2025Article
- Structure and substrate promiscuity of Campylobacter jejuni periplasmic nitrate reductase (Nap) and phylogenetic analysis of Nap homologs.The Journal of biological chemistry · 2025Article
- Molybdenum Cofactor Model Reveals Remarkable Redox Activity at Both Molybdenum and the Pyranopterin Dithiolene Ligand.Journal of the American Chemical Society · 2025Article
- Expanding Perchlorate Use for C-H Oxidative Transformations: A Tandem Photo- and Iron-Catalytic Strategy.Organometallics · 2025Article
- Metatranscriptomics-guided discovery and characterization of a polyphenol-metabolizing gut microbial enzyme.Cell host & microbe · 2024Article
- The Construction of an Extreme Radiation-Resistant Perchlorate-Reducing Bacterium UsingInternational journal of molecular sciences · 2024Article
- The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Metagenomic profiling of halites from the Atacama Desert: an extreme environment with natural perchlorate does not promote high diversity of perchlorate reducing microorganisms.Extremophiles : life under extreme conditions · 2024Article
- Iron-Catalyzed C-H Oxygenation Using Perchlorate Enabled by Secondary Sphere Hydrogen Bonds.Journal of the American Chemical Society · 2024Article
- Review
- Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis.Molecules (Basel, Switzerland) · 2023Review
- Making Moco: A Personal History.Molecules (Basel, Switzerland) · 2023Review
- Chlorine redox chemistry is widespread in microbiology.The ISME journal · 2023Article
- Characterisation of the redox centers of ethylbenzene dehydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
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10 authors.
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Abstract
Perchlorate is an important ion on both Earth and Mars. Perchlorate reductase (PcrAB), a specialized member of the dimethylsulfoxide reductase superfamily, catalyzes the first step of microbial perchlorate respiration, but little is known about the biochemistry, specificity, structure, and mechanism of PcrAB. Here we characterize the biophysics and phylogeny of this enzyme and report the 1.86-Å resolution PcrAB complex crystal structure. Biochemical analysis revealed a relatively high perchlorate affinity (Km = 6 μm) and a characteristic substrate inhibition compared with the highly similar respiratory nitrate reductase NarGHI, which has a relatively much lower affinity for perchlorate (Km = 1.1 mm) and no substrate inhibition. Structural analysis of oxidized and reduced PcrAB with and without the substrate analog SeO3 (2-) bound to the active site identified key residues in the positively charged and funnel-shaped substrate access tunnel that gated substrate entrance and product release while trapping transiently produced chlorate. The structures suggest gating was associated with shifts of a Phe residue between open and closed conformations plus an Asp residue carboxylate shift between monodentate and bidentate coordination to the active site molybdenum atom. Taken together, structural and mutational analyses of gate residues suggest key roles of these gate residues for substrate entrance and product release. Our combined results provide the first detailed structural insight into the mechanism of biological perchlorate reduction, a critical component of the chlorine redox cycle on Earth.
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