UV resonance Raman studies of alpha-nitrosyl hemoglobin derivatives: relation between the alpha 1-beta 2 subunit interface interactions and the Fe-histidine bonding of alpha heme
| ISSN: | 0006-2960 |
|---|---|
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::568a6f3e34fe6f479c32e510184ecce8 https://pubmed.ncbi.nlm.nih.gov/10423244 |
| Přírůstkové číslo: | edsair.doi.dedup.....568a6f3e34fe6f479c32e510184ecce8 |
| Autor: | Teizo Kitagawa, A. Tsuneshige, Masako Nagai, Yonetani T, Shigenori Nagatomo |
| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Phytic Acid Stereochemistry Protein Conformation Ultraviolet Rays Protein subunit Iron Alpha (ethology) Heme Cleavage (embryo) Spectrum Analysis Raman Biochemistry law.invention chemistry.chemical_compound Hemoglobins law Humans Histidine Beta (finance) Electron paramagnetic resonance Chemistry Electron Spin Resonance Spectroscopy Tryptophan Hydrogen Bonding Hydrogen-Ion Concentration Resonance (chemistry) Carboxyhemoglobin Tyrosine |
| Zdroj: | Biochemistry. 38(30) |
| ISSN: | 0006-2960 |
| Popis: | Human alpha-nitrosyl beta-deoxy hemoglobin A, alpha(NO)beta(deoxy), is considered to have a T (tense) structure with the low O(2) affinity extreme and the Fe-histidine (His87) (Fe-His) bond of alpha heme cleaved. The Fe-His bonding of alpha heme and the intersubunit interactions at the alpha 1-beta 2 contact of alpha(NO)-Hbs have been examined under various conditions with EPR and UV resonance Raman (UVRR) spectra excited at 235 nm, respectively. NOHb at pH 6.7 gave the UVRR spectrum of the R structure, but in the presence of inositol-hexakis-phosphate (IHP) for which the Fe-His bond of the alpha heme is broken, UVRR bands of Trp residues behaved half-T-like while Tyr bands remained R-like. The half-ligated nitrosylHb, alpha(NO)beta(deoxy), in the presence of IHP at pH 5.6, gave T-like UVRR spectra for both Tyr and Trp, but binding of CO to its beta heme (alpha(NO)beta(CO)) changed the UVRR spectrum to half-T-like. Binding of NO to its beta heme (NOHb) changed the UVRR spectrum to 70% T-type for Trp but almost R-type for Tyr. When the pH was raised to 8.2 in the presence of IHP, the UVRR spectrum of NOHb was the same as that of COHb. EPR spectra of these Hbs indicated that the Fe-His bond of alpha(NO) heme is partially cleaved. On the other hand, the UVRR spectra of alpha(NO)beta(deoxy) in the absence of IHP at pH 8.8 showed the T-like UVRR spectrum, but the EPR spectrum indicated that 40-50% of the Fe-His bond of alpha hemes was intact. Therefore, it became evident that there is a qualitative correlation between the cleavage of the Fe-His bond of alpha heme and T-like contact of Trp-beta 37. We note that the behaviors of Tyr and Trp residues at the alpha 1-beta 2 interface are not synchronous. It is likely that the behaviors of Tyr residues are controlled by the ligation of beta heme through His-beta 92(F8)-->Val-beta 98(FG5)-->Asp-beta 99(G1 )-->Tyr-alpha 42(C7) or Tyr-beta 145(HC2). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|