ArticleJournal of the American Chemical Society2012
Protein conformational gating of enzymatic activity in xanthine oxidoreductase.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 59 citations in OpenAlex.
- Diet-derived urolithin A is produced by a dehydroxylase encoded by human gut Enterocloster species.Nature communications · 2025Article
- Interaction of Tri-Cyclic Nucleobase Analogs with Enzymes of Purine Metabolism: Xanthine Oxidase and Purine Nucleoside Phosphorylase.International journal of molecular sciences · 2024Article
- Molybdenum's Role as an Essential Element in Enzymes Catabolizing Redox Reactions: A Review.Biomolecules · 2024Review
- Bringing Nitric Oxide to the Molybdenum World-A Personal Perspective.Molecules (Basel, Switzerland) · 2023Review
- Metal-Containing Formate Dehydrogenases, a Personal View.Molecules (Basel, Switzerland) · 2023Review
- Design, synthesis, molecular docking and biological evaluation of new carbazole derivatives as anticancer, and antioxidant agents.BMC chemistry · 2023Article
- Association of Mutations Identified in Xanthinuria with the Function and Inhibition Mechanism of Xanthine Oxidoreductase.Biomedicines · 2021Review
- Article
- Iron-sulfur flavoenzymes: the added value of making the most ancient redox cofactors and the versatile flavins work together.Open biology · 2021Article
- Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms.FEBS open bio · 2019Article
- Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes.Redox biology · 2018Review
- Structure-Activity Relationship of Xanthones as Inhibitors of Xanthine Oxidase.Molecules (Basel, Switzerland) · 2018Article
- A eukaryotic nicotinate-inducible gene cluster: convergent evolution in fungi and bacteria.Open biology · 2017Article
- Electron transfer pathways in a multiheme cytochrome MtrF.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A single nucleotide polymorphism causes enhanced radical oxygen species production by human aldehyde oxidase.PloS one · 2017Article
- Xanthine dehydrogenase: An old enzyme with new knowledge and prospects.Bioengineered · 2016Article
- Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase.Nature chemical biology · 2015Article
- The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase.The FEBS journal · 2015Article
- Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Review
- Proton transfer reactions and hydrogen-bond networks in protein environments.Journal of the Royal Society, Interface · 2014Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
In mammals, xanthine oxidoreductase can exist as xanthine dehydrogenase (XDH) and xanthine oxidase (XO). The two enzymes possess common redox active cofactors, which form an electron transfer (ET) pathway terminated by a flavin cofactor. In spite of identical protein primary structures, the redox potential difference between XDH and XO for the flavin semiquinone/hydroquinone pair (E(sq/hq)) is ~170 mV, a striking difference. The former greatly prefers NAD(+) as ultimate substrate for ET from the iron-sulfur cluster FeS-II via flavin while the latter only accepts dioxygen. In XDH (without NAD(+)), however, the redox potential of the electron donor FeS-II is 180 mV higher than that for the acceptor flavin, yielding an energetically uphill ET. On the basis of new 1.65, 2.3, 1.9, and 2.2 Å resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin. The majority of the E(sq/hq) difference between XDH and XO originates from a conformational change in the loop at positions 423-433 near the flavin binding site, causing the differences in stability of the semiquinone state. There was no large conformational change observed in response to NAD(+) binding at XDH. Instead, the positive charge of the NAD(+) ring, deprotonation of Asp429, and capping of the bulk surface of the flavin by the NAD(+) molecule all contribute to altering E(sq/hq) upon NAD(+) binding to XDH.
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