ArticleThe protein journal2007
Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly.
Article in The protein journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Quantification of Active Apohemoglobin Heme-Binding Sites via Dicyanohemin Incorporation.Biochemistry · 2017Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction between human apohemoglobin A and CN-Mesohemin, a monomeric non-native heme derivative, was probed by Soret spectrophotometric titrations in 0.05 M potassium phosphate buffer, pH 7 at varied temperatures. Hypsochromic shifts in the absorbance maxima were observed at all temperatures below 10 degrees C. First derivative spectroscopy of CN-Mesohemin titrations was used to provide further evidence of a spectral shift upon CN-Mesohemoglobin assembly. Findings of Soret Spectral shifts demonstrate a preference for the alpha chain heme site by CN-Mesohemin indicative of semi-alpha-hemoglobin intermediate formation. CN-Mesohemin, a derivative with peripheral 2,4 ethyl groups, does not possess the extended conjugation seen for native CN-Protohemin with its 2,4 vinyl groups. Indeed, reduced polarity of CN-Mesohemin over that of CN-Protohemin resulted in distinct temperature dependencies. Molecular visualization and protein-ligand interaction analysis targeted a functionally diverse residue unique to the alpha-chain. Tyrosine-42 (a polar/non-polar amino acid) appeared to play a prominent role in the assembly process.
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Registered trials
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