Ligand affinities in mutant metmyoglobins.

doi:10.1016/0167-4838(93)90280-5

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Article

Ligand affinities in mutant metmyoglobins.

Biochimica et biophysica acta - 21 Apr 1993

Biram D, Garratt C J, Hester R E

Abstract excerpt

Ligand binding to the wild-type and a series of mutant porcine myoglobins, expressed and purified from Escherichia coli cells, has been studied using UV-VIS absorption spectroscopy. The proximal pocket mutation, F7 Ser-->Leu (F7), causes an increased affinity for OH- and N3- binding to metmyoglob...

Topics

Animals
Azides
Escherichia coli
Histidine
Hydrogen-Ion Concentration
Ligands
Mutation
Myoglobin
Protein Conformation
Spectrophotometry
Swine
Threonine
Valine

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