title: Differences in coordination states of substituted tyrosine residues and quaternary structures among hemoglobin M probed by resonance Raman spectroscopy.
abstract: Among the four types of hemoglobin (Hb) M with a substitution of a tyrosine (Tyr) for either the proximal (F8) or distal (E7) histidine in the alpha or beta subunits, only Hb M Saskatoon (betaE7Tyr) assumes a hexacoordinate structure and its abnormal subunits can be reduced readily by methemoglobin (metHb) reductase. This is distinct from the other three M Hbs. To gain new insight into the cause of the difference, we examined the ionization states of E7 and F8 Tyrs by UV resonance Raman (RR) spectroscopy and Fe-O(Tyr) bonding by visible RR spectroscopy. Hb M Iwate (alphaF8Tyr), Hb M Boston (alphaE7Tyr), and Hb M Hyde Park (betaF8Tyr) exhibited two extra UV RR bands at 1,603 cm(-1) (Y8a') and 1,167 cm(-1) (Y9a') arising from deprotonated (ionized) Tyr, but Hb M Saskatoon displayed the UV RR bands of protonated (unionized) Tyr at 1,620 and 1,175 cm(-1) in addition to those of deprotonated Tyr. Evidence for the bonding of both ionization states of Tyr to the heme in Hb M Saskatoon was provided by visible RR spectroscopy. These results indicate that betaE7Tyr of Hb M Saskatoon is in equilibrium between protonated and deprotonated forms, which is responsible for facile reducibility. Comparison of the UV RR spectral features of metHb M with that of metHb A has revealed that metHb M Saskatoon and metHb M Hyde Park are in the R (relaxed) structure, similar to that of metHb A, whereas metHb M Iwate, metHb M Boston and metHb M Milwaukee are in the T (tense) quaternary structure.
authors.affiliation: Graduate School of Medical Science, Kanazawa University, Kanazawa, 920-0942, Japan.
authors.forename: Yayoi
authors.initials: Y
authors.lastname: Aki
authors.forename: Masako
authors.initials: M
authors.lastname: Nagai
authors.forename: Yukifumi
authors.initials: Y
authors.lastname: Nagai
authors.forename: Kiyohiro
authors.initials: K
authors.lastname: Imai
authors.forename: Michihiko
authors.initials: M
authors.lastname: Aki
authors.forename: Akira
authors.initials: A
authors.lastname: Sato
authors.forename: Minoru
authors.initials: M
authors.lastname: Kubo
authors.forename: Shigenori
authors.initials: S
authors.lastname: Nagatomo
authors.forename: Teizo
authors.initials: T
authors.lastname: Kitagawa
mesh_terms: D000328:Adult; D019943:Amino Acid Substitution; D001665:Binding Sites; D006449:Hemoglobin M / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D020836:Protein Structure, Quaternary; D013059:Spectrum Analysis, Raman; D013379:Substrate Specificity; D014443:Tyrosine / Q000737:chemistry*
chemical_list: D014443:Tyrosine; D006449:Hemoglobin M
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