1H resonances of proximal histidine in CO complexes of hemoglobins provide a sensitive probe of coordination geometry

FEBS Letters

Dalvit, Claudio¹  Tennant, Linda¹  Wright, Peter E.¹ 

[1] Department of Molecular Biology, Research Institute of Scripps Clinic, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA

关键词: 1H NMR;    Proximal histidine;    Coordination geometry;    Myoglobin;    Leghemoglobin;    Hemoglobin α-subunit;   

DOI  :  10.1016/0014-5793(87)81507-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A straightforward strategy for assignment of the C^ϵH, C^δH and N^δH proton resonances of the proximal histidine ligand in diamagnetic complexes of monomeric hemoglobins and myoglobins is reported. These resonances are subject to large ring current shifts and are highly sensitive to coordination geometry. There are no significant differences between the CO complexes of myoglobin, leghemoglobin or hemoglobin α-subunits in proximal His coordination geometry or hydrogen bonding to the backbone at Leu F4. Ring current calculations show that the His F8 coordination geometry in the CO complexes of myoglobin and hemoglobin α-subunits is very similar in crystal and solution.

【 授权许可】

Unknown