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

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

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Bibliographic Details
Published in:	Biomolecular NMR assignments Vol. 3; no. 2; pp. 211 - 214
Main Authors:	Pond, Matthew P, Vuletich, David A, Falzone, Christopher J, Majumdar, Ananya, Lecomte, Juliette T J
Format:	Journal Article
Language:	English
Published:	Netherlands 01-12-2009
Subjects:	Bacterial Proteins - chemistry Bacterial Proteins - metabolism Heme - metabolism Hemoglobins - chemistry Hemoglobins - metabolism Histidine Iron Nuclear Magnetic Resonance, Biomolecular Protein Processing, Post-Translational Synechococcus
Online Access:	Get full text
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Summary:	The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 is a monomeric 123-residue Group I 2/2 hemoglobin. Here, we report (1)H, (15)N, and (13)C assignments for the ferric (low-spin, S = (1/2)) protein with a b heme cofactor and after post-translational modification leading to a c-like heme.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1874-270X
DOI:	10.1007/s12104-009-9177-1