Active site complementation in engineered heterodimers of Escherichia coli glutathione reductase created in vivo.

doi:10.1098/rspb.1990.0127

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Article

Active site complementation in engineered heterodimers of Escherichia coli glutathione reductase created in vivo.

Proceedings. Biological sciences - 22 Dec 1990

Scrutton N S, Berry A, Deonarain M P, Perham R N

Abstract excerpt

By directed mutagenesis of the cloned Escherichia coli gor gene encoding the dimeric flavoprotein glutathione reductase, Cys-47 (a cysteine residue forming an essential charge-transfer complex with enzyme-bound FAD) was converted to serine (C47S) and His-439 (required to facilitate protonation of...

Topics

Amino Acid Sequence
Binding Sites
Escherichia coli
Genes, Bacterial
Genetic Complementation Test
Glutathione Reductase
Molecular Sequence Data
Mutation
Protein Conformation
Protein Engineering

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