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Cited by 1,470

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Single-Molecule Enzymatic Dynamics

Lu, H. P.·1998·Science

Abstract

Enzymatic turnovers of single cholesterol oxidase molecules were observed in real time by monitoring the emission from the enzyme's fluorescent active site, flavin adenine dinucleotide (FAD). Statistical analyses of single-molecule trajectories revealed a significant and slow fluctuation in the rate of cholesterol oxidation by FAD. The static disorder and dynamic disorder of reaction rates, which are essentially indistinguishable in ensemble-averaged experiments, were determined separately by the real-time single-molecule approach. A molecular memory phenomenon, in which an enzymatic turnover was not independent of its previous turnovers because of a slow fluctuation of protein conformation, was evidenced by spontaneous spectral fluctuation of FAD.

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Metadata

Authors
Lu, H. P.
Venue
Science
Published
1998-12-04
Volume
282
Issue
5395
Pages
1877-1882
ISSN
0036-8075 (ISSN-L)
OpenAlex
W2142337964
Cited by
1,470
References
1
FWCI
32.75
Type
journal article
Language
en
Open access
closed

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Lu, H. P. (1998). Single-Molecule Enzymatic Dynamics. Science. https://doi.org/10.1126/science.282.5395.1877

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