Article
Hybridization of modified-heme reconstitution and distal histidine mutation to functionalize sperm whale myoglobin.
Journal of the American Chemical Society - 21 Jan 2004
Sato Hideaki, Hayashi Takashi, Ando Tsutomu, Hisaeda Yoshio, Ueno Takafumi, Watanabe Yoshihito
Abstract excerpt
To modulate the physiological function of a hemoprotein, most approaches have been demonstrated by site-directed mutagenesis. Replacement of the native heme with an artificial prosthetic group is another way to modify a hemoprotein. However, an alternate method, mutation or heme reconstitution, does not always demonstrate sufficient improvement compared with the native heme enzyme. In the present study, to...
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