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J. Biol. Chem., Vol. 276, Issue 46, 42881-42886, November 16, 2001
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From the Adenosine 5'-phosphosulfate reductase (APR)
catalyzes the two-electron reduction of adenosine 5'-phosphosulfate to
sulfite and AMP, which represents the key step of sulfate assimilation in higher plants. Recombinant APRs from both Lemna minor
and Arabidopsis thaliana were overexpressed in
Escherichia coli and isolated as yellow-brown proteins.
UV-visible spectra of these recombinant proteins indicated the presence
of iron-sulfur centers, whereas flavin was absent. This result was
confirmed by quantitative analysis of iron and acid-labile sulfide,
suggesting a [4Fe-4S] cluster as the cofactor. EPR spectroscopy of
freshly purified enzyme showed, however, only a minor signal at g = 2.01. Therefore, Mössbauer spectra of 57Fe-enriched
APR were obtained at 4.2 K in magnetic fields of up to 7 tesla, which
were assigned to a diamagnetic [4Fe-4S]2+ cluster. This
cluster was unusual because only three of the iron sites exhibited the
same Mössbauer parameters. The fourth iron site gave, because of
the bistability of the fit, a significantly smaller isomer shift or
larger quadrupole splitting than the other three sites. Thus, plant
assimilatory APR represents a novel type of adenosine 5'-phosphosulfate
reductase with a [4Fe-4S] center as the sole cofactor, which is
clearly different from the dissimilatory adenosine
5'-phosphosulfate reductases found in sulfate reducing bacteria.
Plant Adenosine 5'-Phosphosulfate Reductase Is a Novel
Iron-Sulfur Protein*
§,
,,,,,
Institute of Plant Sciences, University of
Bern, CH-3013 Bern, Switzerland, ¶ Fachbereich Biologie,
Universität Konstanz, D-78457 Konstanz, Germany,
Biochemisches Institut, Universität Zürich,
CH-8057 Zürich, Switzerland, ** Institut für
Physik, Medizinische Universität zu Lübeck, D-23538
Lübeck, Germany, Department of
Chemistry, University of Bern, CH-3013 Bern, Switzerland, and
§§ Laboratoire de Biochimie, University of
Neuchâtel, CH-2000 Neuchâtel, Switzerland
*
This work was supported by grants from the Swiss National
Science Foundation, the EU project OPTIMISTICK, and the Körber Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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