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DIMENSIONAL PROBING OF THE ATP BINDING SITE ON FIREFLY LUCIFERASE
Author(s) -
Rosendahl Mary S.,
Leonard Nelson J.,
Deluca Marlene
Publication year - 1982
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1982.tb02659.x
Subject(s) - luciferase , bioluminescence , firefly protocol , luciferin , nucleotide , chemistry , purine , enzyme , substrate (aquarium) , binding site , biophysics , adenosine triphosphate , biochemistry , stereochemistry , biology , zoology , transfection , ecology , gene
— lin ‐Benzoadenosine 5′‐triphosphate has been shown to be an acceptable substrate for light production in the firefly luciferase‐luciferin system. This nucleotide analogue displays strong enzyme binding and a reduced rate of enzyme catalysis compared with ATP. Variation in the color of the bioluminescence emission with /in‐benzo‐ATP compared with ATP suggests that a lateral extension in the purine base induces a change in the conformation of the luciferase and in the environment of the excited light emitter.