ArticleBiochemistry2013
Multistep, eight-electron oxidation catalyzed by the cofactorless oxidase, PqqC: identification of chemical intermediates and their dependence on molecular oxygen.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- In Hyphomicrobium denitrificans Two Related Sulfane-Sulfur Responsive Transcriptional Repressors Regulate Thiosulfate Oxidation and Have a Deep Impact on Nitrate Respiration and Anaerobic Biosyntheses.Molecular microbiology · 2025Article
- Structural Basis for Methine Excision by a Heme Oxygenase-like Enzyme.ACS central science · 2024Article
- Nitrous oxide respiration in acidophilic methanotrophs.Nature communications · 2024Article
- Adaptive evolutionary strategy coupled with an optimized biosynthesis process for the efficient production of pyrroloquinoline quinone from methanol.Biotechnology for biofuels and bioproducts · 2023Article
- RaS-RiPPs in Streptococci and the Human Microbiome.ACS bio & med chem Au · 2022Review
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone.Current opinion in chemical biology · 2020Review
- An Unusual Route forJournal of bacteriology · 2020Article
- Biological pincer complexes.ChemCatChem · 2020Article
- A two-component protease inThe Journal of biological chemistry · 2019Article
- MftD Catalyzes the Formation of a Biologically Active Redox Center in the Biosynthesis of the Ribosomally Synthesized and Post-translationally Modified Redox Cofactor Mycofactocin.Journal of the American Chemical Society · 2019Article
- Moving Through Barriers in Science and Life.Annual review of biochemistry · 2019Article
- Occurrence, function, and biosynthesis of mycofactocin.Applied microbiology and biotechnology · 2019Review
- Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway.Journal of the American Chemical Society · 2019Article
- Methods for Expression, Purification, and Characterization of PqqE, a Radical SAM Enzyme in the PQQ Biosynthetic Pathway.Methods in enzymology · 2018Article
- The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide.Biochemistry · 2016Article
- Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD.The Journal of biological chemistry · 2016Article
- PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway.The Journal of biological chemistry · 2015Article
- Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.Chemical reviews · 2014Review
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The final step of the biosynthesis of prokaryotic cofactor PQQ is catalyzed by PqqC, a cofactorless oxidase that brings about a ring closure and overall eight-electron oxidation of its substrate. Time-dependent acid quenching and subsequent high-performance liquid chromatography separation and mass spectrometric analyses of reaction mixtures were performed to correlate the structures of intermediates with previously observed UV-visible signatures. The reaction is composed of four stepwise oxidations: three steps use O2 as the two-electron acceptor, and the fourth uses hydrogen peroxide (H2O2). The chemical nature of the intermediates, the stoichiometry of the reaction, and their dependence on the oxygen concentration indicate that the third oxidation uses the product, H2O2, from the preceding step to produce water. The last oxidation step can also be studied separately and is a reaction between O2 and PQQH2 trapped in the active site. This oxidation is approximately 10 times slower than the reoxidation of PQQH2 in solution. From the order of the four oxidation steps and their sensitivity to O2 concentration, we propose a progressive closure of the active site as the enzyme proceeds through its catalytic cycle.
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