(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

Matthew P Pond; David A Vuletich; Christopher J Falzone; Ananya Majumdar; Juliette T J Lecomte

doi:10.1007/s12104-009-9177-1

(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

Biomol NMR Assign. 2009 Dec;3(2):211-4. doi: 10.1007/s12104-009-9177-1. Epub 2009 Jun 28.

Authors

Matthew P Pond¹, David A Vuletich, Christopher J Falzone, Ananya Majumdar, Juliette T J Lecomte

Affiliation

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

PMID: 19888693
DOI: 10.1007/s12104-009-9177-1

Abstract

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.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism
Heme / metabolism
Hemoglobins / chemistry*
Hemoglobins / metabolism
Histidine*
Iron*
Nuclear Magnetic Resonance, Biomolecular
Protein Processing, Post-Translational
Synechococcus*

Substances

Bacterial Proteins
Hemoglobins
Heme
Histidine
Iron