Document Detail

'It's hollow': the function of pores within myoglobin.
MedLine Citation:
PMID:  20675544     Owner:  NLM     Status:  MEDLINE    
Despite a century of research, the cellular function of myoglobin (Mb), the mechanism regulating oxygen (O(2)) transport in the cell and the structure-function relationship of Mb remain incompletely understood. In particular, the presence and function of pores within Mb have attracted much recent attention. These pores can bind to Xe as well as to other ligands. Indeed, recent cryogenic X-ray crystallographic studies using novel techniques have captured snapshots of carbon monoxide (CO) migrating through these pores. The observed movement of the CO molecule from the heme iron site to the internal cavities and the associated structural changes of the amino acid residues around the cavities confirm the integral role of the pores in forming a ligand migration pathway from the protein surface to the heme. These observations resolve a long-standing controversy - but how these pores affect the physiological function of Mb poses a striking question at the frontier of biology.
Ayana Tomita; Ulrike Kreutzer; Shin-ichi Adachi; Shin-ya Koshihara; Thomas Jue
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  The Journal of experimental biology     Volume:  213     ISSN:  1477-9145     ISO Abbreviation:  J. Exp. Biol.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-08-02     Completed Date:  2010-11-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0243705     Medline TA:  J Exp Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  2748-54     Citation Subset:  IM    
Department of Chemistry and Materials Science, Tokyo Institute of Technology, Meguro-ku, Tokyo, 152-8551, Japan.
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MeSH Terms
Binding Sites
Crystallography, X-Ray
Heme / chemistry,  metabolism
Models, Molecular
Molecular Dynamics Simulation
Myoglobin / chemistry*,  metabolism
Oxygen / metabolism
Protein Conformation*
Reg. No./Substance:
0/Myoglobin; 14875-96-8/Heme; 7782-44-7/Oxygen

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