Hydrophobic effect drives oxygen uptake in myoglobin via histidine E7
Since the elucidation of the myoglobin (Mb) structure, a histidine residue on the E helix (His-E7) has been proposed to act as a gate with an open or closed conformation controlling access to the active site. Although it is believed that at low pH, the His-E7 gate is in its open conformation, the fu...
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| Autores principales: | , , , , , |
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| Formato: | Artículo publishedVersion |
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2013
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00219258_v288_n9_p6754_Boechi https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219258_v288_n9_p6754_Boechi_oai |
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