Bioluminescence of the Ca(2+)-binding photoprotein, aequorin, after histidine modification.
Modification studies of the 5 histidine residues in aequorin employing site-directed mutagenesis and diethyl pyrocarbonate suggested that His169 may be the site of binding of molecular oxygen in aequorin. The modification of this residue led to complete loss of activity, whereas modification of the remaining 4 histidine residues yielded mutant aequorins with varying bioluminescence activities.
Ohmiya
Y
Y
Osaka Bioscience Institute, Japan.
Tsuji
F I
FI
D000331:Aequorin / Q000737:chemistry*; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D006639:Histidine / Q000737:chemistry; D049449:Luminescence; D016297:Mutagenesis, Site-Directed; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D013329:Structure-Activity Relationship
D002135:Calcium-Binding Proteins; D011994:Recombinant Proteins; D006639:Histidine; D000331:Aequorin; D004047:Diethyl Pyrocarbonate