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Kinetic properties of cobalt—iron hybrid hemoglobins
Author(s) -
Oertle Maja,
Winterhalter Kaspar H.,
Di Iorio Ernesto E.
Publication year - 1983
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(83)80150-1
Subject(s) - cobalt , hemoglobin , heme , chemistry , protein quaternary structure , protein subunit , hemeprotein , stereochemistry , crystallography , biochemistry , inorganic chemistry , enzyme , gene
The replacement of O 2 with CO was studied on cobalt—iron hemoglobin hybrids. Both proto‐ and meso‐cobalt hemes were used for the reconstitution. In the oxy quaternary conformation no difference is observed between α‐ and β‐subunits when only proto hemes are present in the hybrid ( k 4 = 30 s −1 , k′ 4 / l′ 4 = 2.5). If Co‐meso heme is present on the β‐chains the binding properties of the partner subunit are modified ( k′ 4 / l′ 4 = 4).