ArticleProceedings of the National Academy of Sciences of the United States of America2010
Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 50 citations in OpenAlex.
- Standard Sample Preparation for Serial Femtosecond Crystallography.Biomolecules · 2025Review
- Controlling the trans effect induced by nitric oxide and carbon monoxide: H93C myoglobin versus H-NOX sensors and soluble guanylate cyclase.Protein science : a publication of the Protein Society · 2024Article
- The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.Chemical science · 2023Article
- Ultrafast dynamics of heme distortion in the OCommunications chemistry · 2021Article
- Femtosecond X-ray emission study of the spin cross-over dynamics in haem proteins.Nature communications · 2020Article
- Solvent Composition Drives the Rebinding Kinetics of Nitric Oxide to Microperoxidase.Scientific reports · 2018Article
- Implications of short time scale dynamics on long time processes.Structural dynamics (Melville, N.Y.) · 2017Review
- Direct observation of subpicosecond vibrational dynamics in photoexcited myoglobin.Nature chemistry · 2016Article
- NO binding kinetics in myoglobin investigated by picosecond Fe K-edge absorption spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy.Structural dynamics (Melville, N.Y.) · 2015Article
- Tryptophan-to-heme electron transfer in ferrous myoglobins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Motion of proximal histidine and structural allosteric transition in soluble guanylate cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Multiphoton absorption of myoglobin-nitric oxide complex: relaxation by D-NEMD of a stationary state.The journal of physical chemistry. B · 2012Article
- Vibrational coherence spectroscopy of the heme domain in the CO-sensing transcriptional activator CooA.Journal of the American Chemical Society · 2011Article
- Probing the local electronic and geometric properties of the heme iron center in a H-NOX domain.Journal of inorganic biochemistry · 2011Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigated the ultrafast structural transitions of the heme induced by nitric oxide (NO) binding for several heme proteins by subpicosecond time-resolved resonance Raman and femtosecond transient absorption spectroscopy. We probed the heme iron motion by the evolution of the iron-histidine Raman band intensity after NO photolysis. Unexpectedly, we found that the heme response and iron motion do not follow the kinetics of NO rebinding. Whereas NO dissociation induces quasi-instantaneous iron motion and heme doming (<0.6 ps), the reverse process results in a much slower picosecond movement of the iron toward the planar heme configuration after NO binding. The time constant for this primary domed-to-planar heme transition varies among proteins (approximately 30 ps for myoglobin and its H64V mutant, approximately 15 ps for hemoglobin, approximately 7 ps for dehaloperoxidase, and approximately 6 ps for cytochrome c) and depends upon constraints exerted by the protein structure on the heme cofactor. This observed phenomenon constitutes the primary structural transition in heme proteins induced by NO binding.
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