ArticleJournal of the American Chemical Society2005
Temperature-dependent studies of NO recombination to heme and heme proteins.
Article in Journal of the American Chemical Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 90 citations in OpenAlex.
- 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
- 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
- Ultrafast CO Kinetics in Heme Proteins: Adiabatic Ligand Binding and Heavy Atom Tunneling.Journal of the American Chemical Society · 2017Article
- Implications of short time scale dynamics on long time processes.Structural dynamics (Melville, N.Y.) · 2017Review
- From curiosity to applications. A personal perspective on inorganic photochemistry.Chemical science · 2016Review
- 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
- Investigations of the low frequency modes of ferric cytochrome c using vibrational coherence spectroscopy.The journal of physical chemistry. B · 2014Article
- Parallel and competitive pathways for substrate desaturation, hydroxylation, and radical rearrangement by the non-heme diiron hydroxylase AlkB.Journal of the American Chemical Society · 2012Article
- How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase.Antioxidants & redox signaling · 2012Review
- Effect of DNA binding on geminate CO recombination kinetics in CO-sensing transcription factor CooA.The Journal of biological chemistry · 2012Article
- Multiphoton absorption of myoglobin-nitric oxide complex: relaxation by D-NEMD of a stationary state.The journal of physical chemistry. B · 2012Article
- Quaternary structure controls ligand dynamics in soluble guanylate cyclase.The Journal of biological chemistry · 2012Article
- A "sliding scale rule" for selectivity among NO, CO, and O₂ by heme protein sensors.Biochemistry · 2012Article
- Blocking the gate to ligand entry in human hemoglobin.The Journal of biological chemistry · 2011Article
- Molecular probes of the mechanism of cytochrome P450. Oxygen traps a substrate radical intermediate.Archives of biochemistry and biophysics · 2011Article
- CO and O2 binding to pseudo-tetradentate ligand-copper(I) complexes with a variable N-donor moiety: kinetic/thermodynamic investigation reveals ligand-induced changes in reaction mechanism.Journal of the American Chemical Society · 2010Article
- Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- NMR and DFT investigation of heme ruffling: functional implications for cytochrome c.Journal of the American Chemical Society · 2010Article
- Mechanisms of peroxynitrite interactions with heme proteins.Inorganic chemistry · 2010Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
The rebinding kinetics of NO to the heme iron of myoglobin (Mb) is investigated as a function of temperature. Below 200 K, the transition-state enthalpy barrier associated with the fastest (approximately 10 ps) recombination phase is found to be zero and a slower geminate phase (approximately 200 ps) reveals a small enthalpic barrier (approximately 3 +/- 1 kJ/mol). Both of the kinetic rates slow slightly in the myoglobin (Mb) samples above 200 K, suggesting that a small amount of protein relaxation takes place above the solvent glass transition. When the temperature dependence of the NO recombination in Mb is studied under conditions where the distal pocket is mutated (e.g., V68W), the rebinding kinetics lack the slow phase. This is consistent with a mechanism where the slower (approximately 200 ps) kinetic phase involves transitions of the NO ligand into the distal heme pocket from a more distant site (e.g., in or near the Xe4 cavity). Comparison of the temperature-dependent NO rebinding kinetics of native Mb with that of the bare heme (PPIX) in glycerol reveals that the fast (enthalpically barrierless) NO rebinding process observed below 200 K is independent of the presence or absence of the proximal histidine ligand. In contrast, the slowing of the kinetic rates above 200 K in MbNO disappears in the absence of the protein. Generally, the data indicate that, in contrast to CO, the NO ligand binds to the heme iron through a "harpoon" mechanism where the heme iron out-of-plane conformation presents a negligible enthalpic barrier to NO rebinding. These observations strongly support a previous analysis (Srajer et al. J. Am. Chem. Soc. 1988, 110, 6656-6670) that primarily attributes the low-temperature stretched exponential rebinding of MbCO to a quenched distribution of heme geometries. A simple model, consistent with this prior analysis, is presented that explains a variety of MbNO rebinding experiments, including the dependence of the kinetic amplitudes on the pump photon energy.
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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.