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Mutagenesis of the proposed iron‐sulfur cluster binding ligands in Escherichia coli biotin synthase
Author(s) -
Hewitson Kirsty S,
Baldwin Jack E,
Shaw Nicholas M,
Roach Peter L
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01101-7
Subject(s) - biochemistry , cysteine , enzyme , chemistry , iron–sulfur cluster , biotin , formate dehydrogenase , mutant , alanine , mutagenesis , atp synthase , escherichia coli , amino acid , cofactor , gene
Biotin synthase (BioB) is a member of a family of enzymes that includes anaerobic ribonucleotide reductase and pyruvate formate lyase activating enzyme. These enzymes all use S ‐adenosylmethionine during turnover and contain three highly conserved cysteine residues that may act as ligands to an iron‐sulfur cluster required for activity. Three mutant enzymes of BioB have been made, each with one cysteine residue (C53, 57, 60) mutated to alanine. All three mutant enzymes were inactive, but they still exhibited the characteristic UV‐visible spectrum of a [2Fe‐2S] 2+ cluster similar to that of the wild‐type enzyme.