ArticleJournal of computational chemistry2017
Quantum chemical calculations of tryptophan → heme electron and excitation energy transfer rates in myoglobin.
Article in Journal of computational chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 25 citations in OpenAlex.
- Understanding the Mechanism of Triplet-Triplet Energy Transfer in the Photocatalytic [2 + 2] Cycloaddition: Insights From Quantum Chemical Modeling.Journal of computational chemistry · 2025Article
- Excited-State Intramolecular Hydrogen Transfer of Compact Molecules Controls Amyloid Aggregation Profiles.JACS Au · 2022Article
- Photo induced reaction of myoglobins with energy transferred from excited free tryptophan.RSC advances · 2020Article
- Computational analysis of eugenol inhibitory activity in lipoxygenase and cyclooxygenase pathways.Scientific reports · 2020Article
- Brønsted acid catalysis of photosensitized cycloadditions.Chemical science · 2019Article
- Charge migration and charge transfer in molecular systems.Structural dynamics (Melville, N.Y.) · 2017Review
- Quantum chemical calculations of tryptophan → heme electron and excitation energy transfer rates in myoglobin.Journal of computational chemistry · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
The development of optical multidimensional spectroscopic techniques has opened up new possibilities for the study of biological processes. Recently, ultrafast two-dimensional ultraviolet spectroscopy experiments have determined the rates of tryptophan → heme electron transfer and excitation energy transfer for the two tryptophan residues in myoglobin (Consani et al., Science, 2013, 339, 1586). Here, we show that accurate prediction of these rates can be achieved using Marcus theory in conjunction with time-dependent density functional theory. Key intermediate residues between the donor and acceptor are identified, and in particular the residues Val68 and Ile75 play a critical role in calculations of the electron coupling matrix elements. Our calculations demonstrate how small changes in structure can have a large effect on the rates, and show that the different rates of electron transfer are dictated by the distance between the heme and tryptophan residues, while for excitation energy transfer the orientation of the tryptophan residues relative to the heme is important. © 2017 The Authors. Journal of Computational Chemistry Published by Wiley Periodicals, Inc.
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