ArticleThe journal of physical chemistry. B2021
Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Online coupling of size exclusion chromatography to capillary-enhanced Raman spectroscopy for the identification of protein classes in hemolyzed blood serum.Analytical and bioanalytical chemistry · 2025Article
- The discovery of berberine erythrocyte-hemoglobin self-assembly delivery system: a neglected carrier underlying its pharmacokinetics.Drug delivery · 2022Article
- Fluoride binding to characteristic heme-pocket centers: Insights into ligand stability.Journal of inorganic biochemistry · 2021Article
- Raman Spectroscopic Study of TiOMaterials (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The UV-vis absorption, Raman imaging, and resonance Raman (rR) spectroscopy methods were employed to study cyanohemoglobin (HbCN) adducts inside living functional red blood cells (RBCs). The cyanide ligands are especially optically sensitive probes of the active site environment of heme proteins. The rR studies of HbCN and its isotopic analogues (
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Registered trials
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