Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures. | Zendy

Kiyoshi Nagai | Zendy; Teizo Kitagawa | Zendy

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Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures.

Author(s) -

Kiyoshi Nagai,

Teizo Kitagawa

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.4.2033

Subject(s) - valency , protein subunit , beta (programming language) , crystallography , stereochemistry , alpha (finance) , raman spectroscopy , chemistry , physics , biochemistry , gene , medicine , philosophy , linguistics , construct validity , nursing , computer science , optics , patient satisfaction , programming language

Resonance Raman spectra have been obtained of the alpha deoxy and beta deoxy subunits within valency hybrid hemoglobins both in the high-affinity (R) and low-affinity (T) structures. Upon conversion from the R to the T structure, the vibrational frequency of the Fe(II)-N epsilon(His-F8) bond changes from 223 to 207 or 203 cm-1 in the alpha deoxy subunit and from 224 to 220 or 217 cm-1 in the beta deoxy subunit. We estimate that the Fe(II)-N epsilon(His-F8) bond is stretched by the R leads to T transition 3 times more in the alpha subunit (0.024 A) than in the beta subunit (0.0085 A) and, accordingly, the strain energy developed in that bond is 8 times larger in the alpha than in the beta subunit. Hence, the oxygen affinity of the alpha and beta subunits may be regulated by different mechanisms.

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