Article
Electronic control of ligand-binding preference of a myoglobin mutant.
Inorganic chemistry - 2 Sept 2014
Nishimura Ryu, Matsumoto Daichi, Shibata Tomokazu, Yanagisawa Sachiko, Ogura Takashi, Tai Hulin, Matsuo Takashi, Hirota Shun, Neya Saburo, Suzuki Akihiro, Yamamoto Yasuhiko
Abstract excerpt
The L29F mutant of sperm whale myoglobin (Mb), where the leucine 29 residue was replaced by phenylalanine (Phe), was shown to exhibit remarkably high affinity to oxygen (O2), possibly due to stabilization of the heme Fe atom-bound O2 in the mutant protein through a proposed unique electrostatic interaction with the introduced Phe29, in addition to well-known hydrogen bonding with His64 [Carver, T. E.; Brantley,...
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