The distance separating Cys-10 from the high-affinity metal binding site in actin.
The fluorescence resonance energy transfer between 5-[2-[iodoacetyl)amino)ethyl]aminonaphthalene-1-sulphonic acid (1,5-IAEDANS) attached to Cys-10 residue and Co2+ bound to the high affinity metal site was measured. The resonance energy transfer efficiency was 8 +/- 2%, which corresponds to a distance of 2.1 nm using the absorption spectrum of Co-EDTA and 3.0 nm using the more relevant absorption spectrum of Co2+ bound to carboxypeptidase as a model spectrum of Co2+ bound to actin, respectively.
D000199:Actins / Q000378:metabolism*; D001665:Binding Sites; D003035:Cobalt / Q000378:metabolism*; D003545:Cysteine; D005456:Fluorescent Dyes; D007700:Kinetics; D009282:Naphthalenesulfonates; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D000199:Actins; D005456:Fluorescent Dyes; D009282:Naphthalenesulfonates; D003035:Cobalt; C006421:1,5-I-AEDANS; D003545:Cysteine