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Proceedings Paper

Fluorescence studies with malate dehydrogenase from rhizobium japonicum 3I1B-143 bacteroids: a two-tryptophan containing protein
Author(s): Camillo A. Ghiron; Maurice R. Eftink; James K. Waters; David W. Emerich
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Paper Abstract

A number of fluorescence studies, both of trp residues and bound NADH, have been reported for porcine MDH. The large number of trp residues (6) complicates the interpretation of some studies. To circumvent this we have performed studies with a two tryptophan (per subunit) MDH from Rhizobium japonicum 311B-143 bacteroids. We have performed phase/modulation fluorescence lifetime measurements, as a function of temperature and added quencher KI, in order to resolved the 1.3 ns (blue) and 6.6 ns (red) contributions from the two classes of trp residues. Anisotropy decay studies have also been performed. The binding of NADH dynamically quenches the fluorescence of both tip residues, but, unlike mammalian cytoplasmic and mitochondrial MDH, there is not a large enhancement in fluorescence of bound NADH upon forming a ternary complex with either tartronic acid or D-malonate.

Paper Details

Date Published: 1 May 1990
PDF: 5 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17725
Show Author Affiliations
Camillo A. Ghiron, Univ. of Missouri (United States)
Maurice R. Eftink, Univ. of Mississippi (United States)
James K. Waters, Univ. of Missouri (United States)
David W. Emerich, Univ. of Missouri (United States)

Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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