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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 388, Issue 12

Issues

Lumazine proteins from photobacteria: localization of the single ligand binding site to the N-terminal domain

Boris Illarionov
  • 1Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstr. 4, D-85747 Garching, Germany
    On leave of absence from the Institute of Biophysics, 660036 Krasnoyarsk, Russia.
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/ Wolfgang Eisenreich
  • 2Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstr. 4, D-85747 Garching, Germany
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/ Martina Wirth
  • 3Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstr. 4, D-85747 Garching, Germany
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/ Chan Yong Lee / Young Eun Woo / Adelbert Bacher
  • 6Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstr. 4, D-85747 Garching, Germany
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/ Markus Fischer
  • 7Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstr. 4, D-85747 Garching, Germany and Institute of Biochemistry and Food Chemistry, University of Hamburg, Food Chemistry Division, Grindelallee 117, D-20146 Hamburg, Germany
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Published Online: 2007-11-16 | DOI: https://doi.org/10.1515/BC.2007.134

Abstract

Lumazine protein is believed to serve as an optical transponder in bioluminescence emission by certain marine bacteria. Sequence arguments suggest that the protein comprises two similarly folded riboflavin synthase-type domains, but earlier work also suggested that only one domain binds 6,7-dimethyl-8-ribityllumazine (DMRL). We show that the replacement of serine-48 or threonine-50 in the N-terminal domain of lumazine protein of Photobacterium leiognathi modulates the absorbance and fluorescence properties of bound DMRL or riboflavin. Moreover, the replacement of these amino acids is accompanied by reduced ligand affinity. Replacement of serine-48 by tryptophan shifts the 13C NMR signal of the 6-methyl group in bound DMRL upfield by 2.9 ppm as compared to the wild-type protein complex. Replacement of threonine-50 causes a downfield shift of approximately 20 ppm for the 15N NMR signal of N-5, as well as an upfield shift of 3 ppm for the 13C NMR signal of C-7 in bound DMRL, respectively. The replacement of the topologically equivalent serine-144 and proline-146 in the C-terminal domain had no significant impact on optical properties, chemical shifts and apparent binding constants of bound DMRL. These data show that the N-terminal domain is the unique site for ligand binding in lumazine protein.

Keywords: lumazine proteins; nuclear magnetic resonance (NMR) spectroscopy; photobacteria; Photobacterium leiognathi; riboflavin synthase; site-directed mutagenesis

About the article

Corresponding author


Received: 2007-05-10

Accepted: 2007-06-28

Published Online: 2007-11-16

Published in Print: 2007-12-01


Citation Information: Biological Chemistry, Volume 388, Issue 12, Pages 1313–1323, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2007.134.

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