Selective oxidation of methionine beta(55)D6 at the alpha 1 beta 1 interface in hemoglobin completely destabilizes the T-state
When methionine beta(55)D6 in human hemoglobin is oxidized to its sulfoxide derivative, the modified protein appears to maintain most of the chemical and structural properties typical of the native protein. On the contrary, the functional behavior is drastically changed, being characterized (like th...
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Published in | The Journal of biological chemistry Vol. 264; no. 30; p. 17745 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
25.10.1989
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Subjects | |
Online Access | Get full text |
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Summary: | When methionine beta(55)D6 in human hemoglobin is oxidized to its sulfoxide derivative, the modified protein appears to maintain
most of the chemical and structural properties typical of the native protein. On the contrary, the functional behavior is
drastically changed, being characterized (like that of the isolated chains) by high oxygen affinity (p50 = 0.47 torr in 0.1
M Tris (pH 7.3) + 0.1 M NaCl at 25 degrees C), absence of cooperativity (n = 1), and lack of Bohr effect. The complete destabilization
of the T-state as a result of this modification is related to a perturbation of the alpha 1 beta 1 subunit interface, which
in native hemoglobin remains static during the quaternary ligand-linked transition. Results also suggest that methionyl sulfoxide-containing
hemoglobin, obtained under different conditions, assumes functionally different R-states, none of which is exactly comparable
with that typical of the native protein. |
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ISSN: | 0021-9258 1083-351X |