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Structure at 1.0 Å resolution of a high-potential iron–sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus

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Abstract

The aerobic respiratory chain of the thermohalophilic bacterium Rhodothermus marinus, a nonphotosynthetic organism from the Bacteroidetes/Chlorobi group, contains a high-potential iron–sulfur protein (HiPIP) that transfers electrons from a bc 1 analog complex to a caa 3 oxygen reductase. Here, we describe the crystal structure of the reduced form of R. marinus HiPIP, solved by the single-wavelength anomalous diffraction method, based on the anomalous scattering of the iron atoms from the [4Fe–4S]3+/2+ cluster and refined to 1.0 Å resolution. This is the first structure of a HiPIP isolated from a nonphotosynthetic bacterium involved in an aerobic respiratory chain. The structure shows a similar environment around the cluster as the other HiPIPs from phototrophic bacteria, but reveals several features distinct from those of the other HiPIPs of phototrophic bacteria, such as a different fold of the N-terminal region of the polypeptide due to a disulfide bridge and a ten-residue-long insertion.

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Abbreviations

HiPIP:

High-potential iron–sulfur protein

RmHip:

Rhodothermus marinus high-potential iron–sulfur protein

SLS:

Swiss Light Source

Tris:

Tris(hydroxymethyl)aminomethane

Rms:

Root mean square

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Acknowledgments

We are grateful to Nuno A.M. Félix for excellent technical assistance, to Ana Coelho, from the Mass Spectrometry Service of Instituto de Tecnologia Química e Biológica, and to João Carita for cell growth. We thank Carlos Frazão for advice on high-resolution refinement and the European Synchrotron Radiation Facility for provision of synchrotron radiation facilities. X-ray data collection at SLS was supported by the European Commission under the Sixth Framework Programme through the Key Action: Strengthening the European Research Area, Research Infrastructures, contract no. RII3-CT-2004-506008. This work was supported by Fundação para a Ciência e a Tecnologia (PTDC/BIA-PRO/66833/2006 to M.A., POCTI/BIA-PRO/58608/2004 to M.T., REEQ/336/BIO/05, PTDC/BIA-PRO/67105/2006 to A.M.P.M.). M.S. received a grant from Fundação para a Ciência e a Tecnologia (BPD/24193/2005).

Author information

Author notes

  1. Meike Stelter

    Present address: The European Synchrotron Radiation Facility, BP 220, 38043, Grenoble Cedex 9, France

Authors and Affiliations

  1. Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República (EAN), 2780-157, Oeiras, Portugal

    Meike Stelter, Lígia M. Saraiva, Miguel Teixeira & Margarida Archer

  2. Eco-Bio, Instituto de Investigação Científica Tropical, Av. da República (EAN), 2784-505, Oeiras, Portugal

    Ana M. P. Melo

  3. Faculdade de Engenharia e Ciências Naturais, Universidade Lusófona de Humanidades e Tecnologias, Av. do Campo Grande, 376, 1749-024, Lisbon, Portugal

    Ana M. P. Melo

  4. Matis ohf, Gylfaflot 5, 112, Reykjavík, Iceland

    Gudmundur O. Hreggvidsson & Sigridur Hjorleifsdottir

  5. University of Iceland, Askja, Sturlugata 7, 101, Reykjavík, Iceland

    Gudmundur O. Hreggvidsson & Sigridur Hjorleifsdottir

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  1. Meike Stelter
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Corresponding author

Correspondence to Margarida Archer.

Additional information

M. Stelter and A. M. P. Melo contributed equally to this work.

The Rhodothermus marinus high-potential iron–sulfur protein coordinates and structure factors have been deposited in the Protein Data Bank with accession code 3H31.

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Stelter, M., Melo, A.M.P., Hreggvidsson, G.O. et al. Structure at 1.0 Å resolution of a high-potential iron–sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus . J Biol Inorg Chem 15, 303–313 (2010). https://doi.org/10.1007/s00775-009-0603-8

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