Allosteric effects have been observed in the binding of ligands to manganese substituted hemoglobin. Redox measurements indicate a preferred binding of organic phosphates to reduced manganese hemoglobin and the existence of a Bohr effect. The redox n-values, with and without organic phosphate, are similar to those of hemoglobin at all pH values. Differential pH titration of manganese hemoglobin and its nitric oxide derivative demonstrates the existence of both alkaline and acid Bohr effects in the binding of ligands.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 10 1974|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology