Construction of a bisaquo heme enzyme and binding by exogenous ligands.
McRee, D E, Jensen, G M, Fitzgerald, M M, Siegel, H A, Goodin, D B
The crystal structure of the His-175-->Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo...
Construction of a bisaquo heme enzyme and binding by exogenous ligands.
McRee, D E, Jensen, G M, Fitzgerald, M M, Siegel, H A, Goodin, D B
The crystal structure of the His-175-->Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo...
Fitzgerald, M. M., Trester, M. L., Jensen, G. M., McRee, D. E., Goodin, D. B.
The activated state of cytochrome c peroxidase, compound ES, contains a cation radical on the Trp-191 side chain. We recently reported that replacing this tryptophan with glycine creates a buried...