ArticleProceedings of the National Academy of Sciences of the United States of America2015
NO binding kinetics in myoglobin investigated by picosecond Fe K-edge absorption spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Solution phase high repetition rate laser pump x-ray probe picosecond hard x-ray spectroscopy at the Stanford Synchrotron Radiation Lightsource.Structural dynamics (Melville, N.Y.) · 2023Article
- Interplays of electron and nuclear motions along CO dissociation trajectory in myoglobin revealed by ultrafast X-rays and quantum dynamics calculations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Femtosecond X-ray emission study of the spin cross-over dynamics in haem proteins.Nature communications · 2020Article
- Chemical interactions and dynamics with femtosecond X-ray spectroscopy and the role of X-ray free-electron lasers.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019Article
- Solvent Composition Drives the Rebinding Kinetics of Nitric Oxide to Microperoxidase.Scientific reports · 2018Article
- Perspective: Opportunities for ultrafast science at SwissFEL.Structural dynamics (Melville, N.Y.) · 2017Article
- Implications of short time scale dynamics on long time processes.Structural dynamics (Melville, N.Y.) · 2017Review
- Time-resolved X-ray spectroscopies of chemical systems: New perspectives.Structural dynamics (Melville, N.Y.) · 2016Article
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10 authors.
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Abstract
Diatomic ligands in hemoproteins and the way they bind to the active center are central to the protein's function. Using picosecond Fe K-edge X-ray absorption spectroscopy, we probe the NO-heme recombination kinetics with direct sensitivity to the Fe-NO binding after 532-nm photoexcitation of nitrosylmyoglobin (MbNO) in physiological solutions. The transients at 70 and 300 ps are identical, but they deviate from the difference between the static spectra of deoxymyoglobin and MbNO, showing the formation of an intermediate species. We propose the latter to be a six-coordinated domed species that is populated on a timescale of ∼ 200 ps by recombination with NO ligands. This work shows the feasibility of ultrafast pump-probe X-ray spectroscopic studies of proteins in physiological media, delivering insight into the electronic and geometric structure of the active center.
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