The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket

Article ID	Journal	Published Year	Pages	File Type
5152500	Journal of Inorganic Biochemistry	2017	43 Pages	PDF

Abstract

The spectroscopic and functional properties of the single Met80Ala and double Tyr67His/Met80Ala mutants have been investigated in order to gain better insight into the role of Met80-Fe ligation and of the hydrogen bonding network, which also involves Tyr67, in the structure and function of human cytochrome c.211

Keywords

SDS CT1 Cyt C PBS Charge transfer Resonance Raman circular dichroism Site directed mutagenesis sodium dodecyl sulfate cytochrome c Ligand binding kinetics peroxidase activity Elephant Phosphate-buffered saline Myoglobin Sperm whale wild type High spin Low spin Cardiolipin

Related Topics

Physical Sciences and Engineering Chemistry Inorganic Chemistry

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The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket

Authors

Chiara Ciaccio, Lorenzo Tognaccini, Theo Battista, Manuela Cervelli, Barry D. Howes, Roberto Santucci, Massimo Coletta, Paolo Mariottini, Giulietta Smulevich, Laura Fiorucci,