ArticleJournal of the American Chemical Society2011
Oxygen reactivity in flavoenzymes: context matters.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 74 citations in OpenAlex.
- Elucidating the Role of OACS environmental Au · 2024Article
- Quantitative measurements of reactive oxygen species partitioning in electron transfer flavoenzyme magnetic field sensing.Frontiers in physiology · 2024Article
- Spin Dynamics of Flavoproteins.International journal of molecular sciences · 2023Review
- Catalytic mechanism of ancestral L-lysine oxidase assigned by sequence data mining.The Journal of biological chemistry · 2021Article
- Engineering the Turnover Stability of Cellobiose Dehydrogenase toward Long-Term Bioelectronic Applications.ACS sustainable chemistry & engineering · 2021Article
- Rational Redesign of Monoamine Oxidase A into a Dehydrogenase to Probe ROS in Cardiac Aging.ACS chemical biology · 2020Article
- N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.Frontiers in molecular biosciences · 2020Review
- Flavins Act as a Critical Liaison Between Metabolic Homeostasis and Oxidative Stress in the Retina.Frontiers in cell and developmental biology · 2020Review
- A complete bioconversion cascade for dehalogenation and denitration by bacterial flavin-dependent enzymes.The Journal of biological chemistry · 2018Article
- Enzymatic control of dioxygen binding and functionalization of the flavin cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The distribution and mechanism of iodotyrosine deiodinase defied expectations.Archives of biochemistry and biophysics · 2017Review
- Beyond ferryl-mediated hydroxylation: 40 years of the rebound mechanism and C-H activation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Monooxygenase Substrates Mimic Flavin to Catalyze Cofactorless Oxygenations.The Journal of biological chemistry · 2016Article
- The Oxygen Dilemma: A Severe Challenge for the Application of Monooxygenases?Chembiochem : a European journal of chemical biology · 2016Review
- Single Amino Acid Switch between a Flavin-Dependent Dehalogenase and Nitroreductase.Journal of the American Chemical Society · 2015Article
- Reaction of pyranose dehydrogenase from Agaricus meleagris with its carbohydrate substrates.The FEBS journal · 2015Article
- Structure of DnmZ, a nitrososynthase in the Streptomyces peucetius anthracycline biosynthetic pathway.Acta crystallographica. Section F, Structural biology communications · 2015Article
- A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate.The Journal of biological chemistry · 2015Article
- Effect of elevated oxygen concentration on bacteria, yeasts, and cells propagated for production of biological compounds.Microbial cell factories · 2014Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Many flavoenzymes--oxidases and monooxygenases--react faster with oxygen than free flavins do. There are many ideas on how enzymes cause this. Recent work has focused on the importance of a positive charge near N5 of the reduced flavin. Fructosamine oxidase has a lysine near N5 of its flavin. We measured a rate constant of 1.6 × 10(5) M(-1) s(-1) for its reaction with oxygen. The Lys276Met mutant reacted with a rate constant of 291 M(-1) s(-1), suggesting an important role for this lysine in oxygen activation. The dihydroorotate dehydrogenases from E. coli and L. lactis also have a lysine near N5 of the flavin. They react with O(2) with rate constants of 6.2 × 10(4) and 3.0 × 10(3) M(-1) s(-1), respectively. The Lys66Met and Lys43Met mutant enzymes react with rate constants that are nearly the same as those for the wild-type enzymes, demonstrating that simply placing a positive charge near N5 of the flavin does not guarantee increased oxygen reactivity. Our results show that the lysine near N5 does not exert an effect without an appropriate context; evolution did not find only one mechanism for activating the reaction of flavins with O(2).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.