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Mutant hemoglobin stability depends upon location and nature of single point mutation
Author(s) -
Smith Michael L.,
Hjortsberg Kerstin,
Romeo Paul-Henri,
Rosa Jean,
Paul Karl-Gustav
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80307-5
Subject(s) - heme , mutant , point mutation , hemoglobin , methemoglobin , mutation , chemistry , hemeprotein , biochemistry , biophysics , biology , gene , enzyme
The temperature dependence of the rates of heme release from the β subunits of methemoglobin A and 5 β mutant methemoglobins has been determined. The rates were largest fort wo hemoglobins with mutations distal to heme, previously known to be unstable. The other 3 mutants also released heme faster than A. These hemoglobins, with single point mutations at the α 1 β 2 interface, were previously thought to be stable. The low reported yields of the 5 mutant protein covaries with the relative rates of heme release from the met species.