Abstract
Abstract The influence of a single amide group located in the heme active site of Pseudomonas aeruginosa cytochrome c551 on its redox potential (E°′) has been characterized through amino acid substitution of Asn64 with Gln or Ala. The E°′ variation of ca. 60 mV among the proteins is attributed mainly to the alteration of the thermodynamic stability of the oxidized protein by the dipole and hydrogen-bonding ability of the amide group.
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