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- W2135143831 abstract "Dioxygen (O 2 ) and other gas molecules have a fundamental role in a variety of enzymatic reactions. However, it is only poorly understood which O 2 uptake mechanism enzymes employ to promote efficient catalysis and how general this is. We investigated O 2 diffusion pathways into monooxygenase and oxidase flavoenzymes, using an integrated computational and experimental approach. Enhanced-statistics molecular dynamics simulations reveal spontaneous protein-guided O 2 diffusion from the bulk solvent to preorganized protein cavities. The predicted protein-guided diffusion paths and the importance of key cavity residues for oxygen diffusion were verified by combining site-directed mutagenesis, rapid kinetics experiments, and high-resolution X-ray structures. This study indicates that monooxygenase and oxidase flavoenzymes employ multiple funnel-shaped diffusion pathways to absorb O 2 from the solvent and direct it to the reacting C4a atom of the flavin cofactor. The difference in O 2 reactivity among dehydrogenases, monooxygenases, and oxidases ultimately resides in the fine modulation of the local environment embedding the reactive locus of the flavin." @default.
- W2135143831 created "2016-06-24" @default.
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- W2135143831 date "2009-06-30" @default.
- W2135143831 modified "2023-10-12" @default.
- W2135143831 title "Multiple pathways guide oxygen diffusion into flavoenzyme active sites" @default.
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- W2135143831 doi "https://doi.org/10.1073/pnas.0903809106" @default.
- W2135143831 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2698890" @default.
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