ArticleThe protein journal2006
Soret spectral and bioinformatic approaches provide evidence for a critical role of the alpha -subunit in assembly of tetrameric hemoglobin.
Article in The protein journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Quantification of Active Apohemoglobin Heme-Binding Sites via Dicyanohemin Incorporation.Biochemistry · 2017Article
- Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly.The protein journal · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Soret spectral contributions of the alpha-subunit heme pocket have been evaluated by performing static titrations of apohemoglobin A with CNProtohemin under varied experimental conditions. Increasing the temperature from 5 to 30 degrees C in 0.05 M potassium phosphate buffer, pH 7, resulted in a decreasingly prominent hypsochromic shifts reflecting altered the vinyl-globin interactions. Studies at 10 degrees C in over pH range of 6.7-8.0 revealed a profile for the spectral shifts approximating the side chain pK value (7.4) a histidyl residue. These overall spectral changes correspond to DeltaE of < or = 7 kJ/mol indicative of electrostatic noncovalent interactions. Further our current molecular modeling studies indicate that the spatial arrangement and critical noncovalent interactions of tyrosine 42 and histidine 45 (aromatic residues unique to the alpha-subunit) make significant contribution to the Soret spectra. Most interestingly, phylogenetic analyses have revealed the presence of a histidyl triad in the alpha-chain of all vertebrates that form heterotetramers.
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