Plant Adenosine 5′-phosphosulfate Reductase Is a Novel Iron-Sulfur Protein

Kopriva, Stanislav; Büchert, Thomas; Fritz, Günter; Suter, Marianne; Weber, Markus; Benda, Rüdiger; Schaller, Johann; Feller, Urs; Schürmann, Peter; Schünemann, Volker; Trautwein, Alfred X.; Kroneck, Peter M. H.; Brunold, Christian (2001). Plant Adenosine 5′-phosphosulfate Reductase Is a Novel Iron-Sulfur Protein. Journal of biological chemistry, 276(46), pp. 42881-42886. American Society for Biochemistry and Molecular Biology 10.1074/jbc.M107424200

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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 minorand Arabidopsis thaliana were overexpressed inEscherichia 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-4S2+ 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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) > Stress Physiology (discontinued)
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) > Plant nutrition (discontinued)
08 Faculty of Science > Departement of Chemistry and Biochemistry
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS)

UniBE Contributor:

Suter, Marianne; Schaller, Johann; Feller, Urs and Brunold, Christian

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry
500 Science > 580 Plants (Botany)

ISSN:

0021-9258

Publisher:

American Society for Biochemistry and Molecular Biology

Language:

English

Submitter:

Peter Alfred von Ballmoos-Haas

Date Deposited:

25 Apr 2016 09:59

Last Modified:

14 Nov 2017 16:20

Publisher DOI:

10.1074/jbc.M107424200

PubMed ID:

11553635

BORIS DOI:

10.7892/boris.81039

URI:

https://boris.unibe.ch/id/eprint/81039

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