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1H, 15N, and 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state

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Abstract

The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 is a monomeric 123-residue Group I 2/2 hemoglobin. Here, we report 1H, 15N, and 13C assignments for the ferric (low-spin, S = ½) protein with a b heme cofactor and after post-translational modification leading to a c-like heme.

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Acknowledgments

The authors thank Nancy Scott and Yagmur Muftuoglu for assistance with protein preparation and Matthew Preimesberger for pH dependence data. This work was supported by NASA grant NNG04GN33H (DAV) and National Science Foundation Grants MCB-0349409 and MCB-0804005.

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Author notes

  1. David A. Vuletich

    Present address: Department of Biomedical Engineering, University of Alberta, Edmonton, AB, T6G 2V2, Canada

Authors and Affiliations

  1. T.C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD, 21218, USA

    Matthew P. Pond & Juliette T. J. Lecomte

  2. Department of Chemistry, The Pennsylvania State University, University Park, PA, 16802, USA

    David A. Vuletich

  3. Department of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA

    Christopher J. Falzone

  4. Biomolecular NMR Center, Johns Hopkins University, Baltimore, MD, 21218, USA

    Ananya Majumdar

Authors
  1. Matthew P. Pond
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  2. David A. Vuletich
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  3. Christopher J. Falzone
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  4. Ananya Majumdar
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  5. Juliette T. J. Lecomte
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Corresponding author

Correspondence to Juliette T. J. Lecomte.

Additional information

Matthew P. Pond and David A. Vuletich contributed equally to this work.

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Pond, M.P., Vuletich, D.A., Falzone, C.J. et al. 1H, 15N, and 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state. Biomol NMR Assign 3, 211–214 (2009). https://doi.org/10.1007/s12104-009-9177-1

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  • DOI: https://doi.org/10.1007/s12104-009-9177-1

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