Geodesic
Cyanide dissociation from ferrous myoglobins: a possible role for the distal histidine
Atti della Accademia nazionale dei Lincei. Rendiconti della Classe di scienze fisiche, matematiche e naturali, Série 8, Tome 83 (1989) no. 1, pp. 287-292 Cet article a éte moissonné depuis la source Biblioteca Digitale Italiana di Matematica

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The reduction of cyanide saturated met myoglobin proceeds via a two step mechanism in which an unstable intermediate species, identified as cyanide bound ferrous myoglobin, is rapidly formed and decays slowly to the final species, unliganded ferrous myoglobin. Both reactions were investigated by time resolved optical spectroscopy in two myoglobins (from horse heart and Aplysia limacina buccal muscle) which differ from one another in many amino acid substitutions, but in particular because one of them (Aplysia I.) lacks the almost invariant distal histidine residue (E7). The different functional behaviour of the two proteins allows us to suggest a molecular mechanism for the dissociation of cyanide involving a «catalytic» role of proton transfer from the distal histidine to the bound cyanide ion. 
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     title = {Cyanide dissociation from ferrous myoglobins: a possible role for the distal histidine},
     journal = {Atti della Accademia nazionale dei Lincei. Rendiconti della Classe di scienze fisiche, matematiche e naturali},
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Brunori, Maurizio; Bellelli, Andrea; Antonini, Giovanni. Cyanide dissociation from ferrous myoglobins: a possible role for the distal histidine. Atti della Accademia nazionale dei Lincei. Rendiconti della Classe di scienze fisiche, matematiche e naturali, Série 8, Tome 83 (1989) no. 1, pp. 287-292. http://geodesic.mathdoc.fr/item/RLINA_1989_8_83_1_a40/

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