Probing the caspase-3 active site by fluorescence lifetime measurements.
The active site of an apoptotic enzyme caspase-3 was characterized by measuring the intrinsic fluorescence of two tryptophan residues. Temperature dependence of the intrinsic fluorescence, the energy homotransfer between the tryptophan residues, and the fluorescence quenching by tetrapeptide inhibitors were investigated by the fluorescence lifetime measurements. It has been observed that the fluorescence lifetimes of caspase-3 in complex with inhibitors were significantly shortened by the electron transfer process.
Kyoung
Minjoung
M
Division of Molecular Life Sciences and Department of Chemistry, Ewha Womans University, Seoul, South Korea.
Kim
So Yeon
SY
Seok
Hee-Young
HY
Park
Il-Sun
IS
Lee
Minyung
M
D053148:Caspase 3; D020169:Caspases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D007700:Kinetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods; D014364:Tryptophan / Q000032:analysis
D015853:Cysteine Proteinase Inhibitors; D011994:Recombinant Proteins; D014364:Tryptophan; D053148:Caspase 3; D020169:Caspases