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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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