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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| Authors: | Matthew P. Pond David A. Vuletich Christopher J. Falzone Ananya Majumdar Juliette T. J. Lecomte |
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| Affiliation: | (1) T.C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA;(2) Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA;(3) Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA;(4) Biomolecular NMR Center, Johns Hopkins University, Baltimore, MD 21218, USA;(5) Present address: Department of Biomedical Engineering, University of Alberta, Edmonton, AB, T6G 2V2, Canada; |
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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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