ArticleProceedings of the National Academy of Sciences of the United States of America2015
Tryptophan-to-heme electron transfer in ferrous myoglobins.
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 8 papers.
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Who cites it
8 citing papers in PubMed.
- Unveiling an Ultrareduced State of Heme in Myoglobin.Journal of the American Chemical Society · 2025Article
- Development of a TSR-based method for understanding structural relationships of cofactors and local environments in photosystem I.BMC bioinformatics · 2025Article
- Solanum lycopersicum heme-binding protein 2 as a potent antimicrobial weapon against plant pathogens.Scientific reports · 2023Article
- Heme Protein Binding of Sulfonamide Compounds: A Correlation Study by Spectroscopic, Calorimetric, and Computational Methods.ACS omega · 2022Article
- Photo induced reaction of myoglobins with energy transferred from excited free tryptophan.RSC advances · 2020Article
- Charge migration and charge transfer in molecular systems.Structural dynamics (Melville, N.Y.) · 2017Review
- Implications of short time scale dynamics on long time processes.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
5 authors.
Funding
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Abstract
It was recently demonstrated that in ferric myoglobins (Mb) the fluorescence quenching of the photoexcited tryptophan 14 (*Trp(14)) residue is in part due to an electron transfer to the heme porphyrin (porph), turning it to the ferrous state. However, the invariance of *Trp decay times in ferric and ferrous Mbs raises the question as to whether electron transfer may also be operative in the latter. Using UV pump/visible probe transient absorption, we show that this is indeed the case for deoxy-Mb. We observe that the reduction generates (with a yield of about 30%) a low-valence Fe-porphyrin π [Fe(II)(porph(●-))] -anion radical, which we observe for the first time to our knowledge under physiological conditions. We suggest that the pathway for the electron transfer proceeds via the leucine 69 (Leu(69)) and valine 68 (Val(68)) residues. The results on ferric Mbs and the present ones highlight the generality of Trp-porphyrin electron transfer in heme proteins.
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