ArticleJournal of the American Chemical Society2010
New light on NO bonding in Fe(III) heme proteins from resonance Raman spectroscopy and DFT modeling.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
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- A Tale of Two Cities in Fluorescent Sensing of Carbon Monoxide: Probes That Detect CO and Those That Detect Only Chemically Reactive CO Donors (CORMs), but Not CO.The Journal of organic chemistry · 2024Review
- Bio-Inspired Imprinting Materials for Biomedical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Insights into the effect of distal histidine and water hydrogen bonding on NO ligation to ferrous and ferric heme: a DFT study.RSC advances · 2022Article
- Exploring the Limits of Dative Boratrane Bonding: Iron as a Strong Lewis Base in Low-Valent Non-Heme Iron-Nitrosyl Complexes.Inorganic chemistry · 2020Article
- Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020Article
- Biological and Bioinspired Inorganic N-N Bond-Forming Reactions.Chemical reviews · 2020Review
- Alternative modes of OJournal of inorganic biochemistry · 2020Article
- Discovery of a Nitric Oxide-Responsive Protein inMolecules (Basel, Switzerland) · 2019Article
- Anharmonic Vibrational Analysis of Biomolecules and Solvated Molecules Using Hybrid QM/MM Computations.Journal of chemical theory and computation · 2019Article
- Mechanisms of HNO Reactions with Ferric Heme Proteins.Angewandte Chemie (International ed. in English) · 2018Article
- Article
- Comprehensive Fe-ligand vibration identification in {FeNO}6 hemes.Journal of the American Chemical Society · 2014Article
- Fourier transform infrared spectroscopy study of ligand photodissociation and migration in inducible nitric oxide synthase.F1000Research · 2014Article
- pH-dependent picosecond structural dynamics in the distal pocket of nitrophorin 4 investigated by 2D IR spectroscopy.The journal of physical chemistry. B · 2013Article
- Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding.Physical chemistry chemical physics : PCCP · 2013Article
- Electronic structure and ligand vibrations in FeNO, CoNO, and FeOO porphyrin adducts.Inorganic chemistry · 2013Article
- Two-Dimensional Stimulated Ultraviolet Resonance Raman Spectra of Tyrosine and Tryptophan; A Simulation Study.Journal of Raman spectroscopy : JRS · 2013Article
- CO, NO and OCoordination chemistry reviews · 2013Article
- 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
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5 authors.
Funding
Abstract
Visible and ultraviolet resonance Raman (RR) spectra are reported for Fe(III)(NO) adducts of myoglobin variants with altered polarity in the distal heme pockets. The stretching frequencies of the Fe(III)-NO and N-O bonds, nu(FeN) and nu(NO), are negatively correlated, consistent with backbonding. However, the correlation shifts to lower nu(NO) for variants lacking a distal histidine. DFT modeling reproduces the shifted correlations and shows the shift to be associated with the loss of a lone-pair donor interaction from the distal histidine that selectively strengthens the N-O bond. However, when the model contains strongly electron-withdrawing substituents at the heme beta-positions, nu(FeN) and nu(NO) become positively correlated. This effect results from Fe(III)-N-O bending, which is induced by lone-pair donation to the N(NO) atom. Other mechanisms for bending are discussed, which likewise lead to a positive nu(FeN)/nu(NO) correlation, including thiolate ligation in heme proteins and electron-donating meso-substituents in heme models. The nu(FeN)/nu(NO) data for the Fe(III) complexes are reporters of heme pocket polarity and the accessibility of lone pair, Lewis base donors. Implications for biologically important processes, including NO binding, reductive nitrosylation, and NO reduction, are discussed.
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