THE STOICHIOMETRY OF BINDING OF FLAVIN MONONUCLEOTIDE (FMN) HYDROQUINONE TO ESCHERICHIA-COLI CHORISMATE SYNTHASE

Authors
RAMJEE MK COGGINS JR HAWKES TR LOWE DJ THORNELEY RNF
Citation
Mk. Ramjee et al., THE STOICHIOMETRY OF BINDING OF FLAVIN MONONUCLEOTIDE (FMN) HYDROQUINONE TO ESCHERICHIA-COLI CHORISMATE SYNTHASE, Bioorganic & medicinal chemistry letters, 3(7), 1993, pp. 1409-1414
Citations number
17
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
3
Issue
7
Year of publication
1993
Pages
1409 - 1414
Database
ISI
SICI code
0960-894X(1993)3:7<1409:TSOBOF>2.0.ZU;2-Q
Abstract
Escherichia coli chorismate synthase (EC 4.6.1.4), purified aerobicall y, does not contain oxidised flavin mononucleotide (FMN) as judged by its uv/visible and fluorescence spectra. However, transient kinetic st udies of functioning enzyme show that each enzyme tetramer binds four equivalents of FMNH2, the reduced hydroquinone state. The higher affin ity of chorismate synthase for FMNH2 (K(D) < 2 muM) relative to FMN (K (D) > 20 muM) is similar to that of bacterial luciferase.