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A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus.

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Title: A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus.
Authors: Bolton R; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom., Machelett MM; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.; National Oceanography Centre, Southampton SO14 3ZH, United Kingdom., Stubbs J; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom., Axford D; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom., Caramello N; European Synchrotron Radiation Facility, Grenoble Cedex 9 38043, France.; Hamburg Centre for Ultrafast Imaging, Hamburg Advanced Research Centre for Bioorganic Chemistry, Universität Hamburg, Hamburg 22761, Germany., Catapano L; Randall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, London SE1 1UL, United Kingdom.; Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom., Malý M; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom., Rodrigues MJ; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom.; Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland., Cordery C; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom., Tizzard GJ; School of Chemistry, University of Southampton, Southampton SO17 1BJ, United Kingdom., MacMillan F; School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom., Engilberge S; European Synchrotron Radiation Facility, Grenoble Cedex 9 38043, France.; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble Cedex 9 38044, France., von Stetten D; European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22607, Germany., Tosha T; Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center, Sayo, Hyogo 679-5148, Japan., Sugimoto H; Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center, Sayo, Hyogo 679-5148, Japan., Worrall JAR; School of Life Sciences, University of Essex, Colchester CO4 3SQ, United Kingdom., Webb JS; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.; National Biofilms Innovation Centre (NBIC), University of Southampton, Southampton, SO17 3DF, UK., Zubkov M; National Oceanography Centre, Southampton SO14 3ZH, United Kingdom.; Scottish Association for Marine Science, Oban, Scotland PA37 1QA, United Kingdom., Coles S; School of Chemistry, University of Southampton, Southampton SO17 1BJ, United Kingdom., Mathieu E; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble Cedex 9 38044, France., Steiner RA; Randall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, London SE1 1UL, United Kingdom.; Department of Biomedical Sciences, University of Padova, Padova 35131, Italy., Murshudov G; Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom., Schrader TE; Forschungszentrum Jülich GmbH, Jülich Centre for Neutron Science, Garching 85748, Germany., Orville AM; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom.; Research Complex at Harwell, Harwell Science and Innovation Campus, Didcot OX11 0FA, United Kingdom Rosalind Franklin Institute, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0QX, United Kingdom., Royant A; European Synchrotron Radiation Facility, Grenoble Cedex 9 38043, France.; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble Cedex 9 38044, France., Evans G; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom.; Rosalind Franklin Institute, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0QX, United Kingdom., Hough MA; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom.; School of Life Sciences, University of Essex, Colchester CO4 3SQ, United Kingdom.; Research Complex at Harwell, Harwell Science and Innovation Campus, Didcot OX11 0FA, United Kingdom Rosalind Franklin Institute, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0QX, United Kingdom., Owen RL; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, United Kingdom., Tews I; Biological Sciences, Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.
Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Mar 19; Vol. 121 (12), pp. e2308478121. Date of Electronic Publication: 2024 Mar 15.
Publication Type: Journal Article
Journal Info: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
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  Data: A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus.
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