ArticleChemistry & biodiversity2012
Correlating C-H bond cleavage with molybdenum reduction in xanthine oxidase.
Article in Chemistry & biodiversity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Investigation of the Inhibition Mechanism of Xanthine Oxidoreductase by Oxipurinol: A Computational Study.Journal of chemical information and modeling · 2023Article
- Computational Characterization of the Inhibition Mechanism of Xanthine Oxidoreductase by Topiroxostat.ACS catalysis · 2023Article
- Xanthine oxidase-product complexes probe the importance of substrate/product orientation along the reaction coordinate.Dalton transactions (Cambridge, England : 2003) · 2017Article
- The mononuclear molybdenum enzymes.Chemical reviews · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We have performed a computational study of substrate C-H bond activation in enzymes of the XO family. The C-H H-atom for all XO substrates studied is transferred to the terminal sulfido at the transition state with near neutral charge, and this is consistent with both Mo=S π→ C-H σ* and C-H σ→Mo=S π* donor-acceptor interactions activating the C-H bond. A C-H bond scission and Mo reduction appear to be highly correlated along the reaction coordinate for all XO substrates studied, with Mo reduction being a continuous and exponential function of C-H bond breaking along the reaction coordinate.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.