Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins.
Logan, D T
Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins. [electronic resource] - Biochemistry Jul 1998 - 10798-807 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-2960
10.1021/bi9806403 doi
Alanine--genetics
Apoenzymes--chemistry
Catalysis
Crystallization
Crystallography, X-Ray
Ferrous Compounds--chemistry
Glutamic Acid--genetics
Hydroxylation
Iron--chemistry
Models, Molecular
Mutagenesis, Site-Directed
Oxygen--chemistry
Phenylalanine--analogs & derivatives
Ribonucleotide Reductases--chemistry
Tyrosine--genetics
Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins. [electronic resource] - Biochemistry Jul 1998 - 10798-807 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-2960
10.1021/bi9806403 doi
Alanine--genetics
Apoenzymes--chemistry
Catalysis
Crystallization
Crystallography, X-Ray
Ferrous Compounds--chemistry
Glutamic Acid--genetics
Hydroxylation
Iron--chemistry
Models, Molecular
Mutagenesis, Site-Directed
Oxygen--chemistry
Phenylalanine--analogs & derivatives
Ribonucleotide Reductases--chemistry
Tyrosine--genetics