PMID: 8950376Nov 12, 1996Paper

Glutamate 94 of [2Fe-2S]-ferredoxins is important for efficient electron transfer in the 1:1 complex formed with ferredoxin-glutamate synthase (GltS) from Synechocystis sp. PCC 6803

Biochimica Et Biophysica Acta
S SchmitzH Böhme

Abstract

We have analyzed the role of critical amino acid residues involved in the interaction between ferredoxin and ferredoxin-glutamate synthase (GOGAT) encoded by the gltS gene from the cyanobacterium Synechocystis sp. PCC 6803. Our results indicated that the glutamate 94 residue of Anabaena 7120 ferredoxin (= E92 of the Synechocystis 6803 ferredoxin) was necessary for an efficient electron transfer to GOGAT comparable to ferredoxin:NADP-reductase, nitrite reductase and nitrate reductase [Schmitz and Böhme (1995) Biochim. Biophys. Acta 1231, 335-341]. The K(m) value determined for wt-ferredoxins and mutant E94Q (and E92Q) was 1 muM, respectively, and activity loss of E94Q was due to a lowered Vmax. Exchange of residue F65 for aliphatic substitutions, which was crucial to electron transfer to ferredoxin:NADP-reductase and nitrite reductase, exhibited only small effects on glutamate synthase-dependent activity while heterocyst ferredoxin and flavodoxin were almost inactive as electron donors. In contrast to data reported for the spinach system, the stoichiometry of the cross-linked complex between ferredoxin and glutamate synthase was 1:1.

References

May 10, 1979·Biochimica Et Biophysica Acta·G ZanettiB Curti
Apr 10, 1992·Biochimica Et Biophysica Acta·M HirasawaD B Knaff
Jan 22, 1991·Biochimica Et Biophysica Acta·D B Knaff, M Hirasawa
Jan 12, 1990·European Journal of Biochemistry·J SanchoC Gómez-Moreno
May 18, 1994·Biochimica Et Biophysica Acta·M HirasawaD B Knaff
Jun 1, 1989·Plant Molecular Biology·H Böhme, R Haselkorn

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Citations

Jun 24, 2011·Bioresource Technology·Martin WinklerThomas Happe
Feb 12, 2004·Biochimica Et Biophysica Acta·Masakazu HirasawaDavid B Knaff
Nov 20, 1997·Biochimica Et Biophysica Acta·A AlivertiG Zanetti

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