Conformation coupled enzyme catalysis: single-molecule and transient kinetics investigation of dihydrofolate reductase.
Authors:Antikainen NM, Smiley RD, Benkovic SJ, Hammes GG
Journal:Biochemistry
PubMed ID:16363797
'Ensemble kinetics and single-molecule fluorescence microscopy were used to study conformational transitions associated with enzyme catalysis by dihydrofolate reductase (DHFR). The active site loop of DHFR was labeled with a fluorescence quencher, QSY35, at amino acid position 17, and the fluorescent probe, Alexa555, at amino acid 37, by introducing cysteines ... More