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Myoglobin engineering

Extensive myoglobin engineering work supports a major role for the distal His in stabilizing the oxy complex relative to the CO complex (182). O2 is a more polar molecule than CO and hence will interact more favorably with neighboring polar groups such as the distal His. This explanation is supported by theoretical work showing that even if CO does tilt or bend, the energetic cost is minimal (184), while the oxy... [Pg.279]

After the completion of this chapter, a review paper on engineering and prosthetic group modification of myoglobin was published (110). The Mb mutant T67R/S92D Mb, which has been briefly reviewed in this chapter (108), was intensively reviewed in this paper. [Pg.488]

Roncone R, Monzani E, Labo S, Sanangelantoni AM, Casella L (2005) Catalytic activity, stability and unfolding of engineered and reconstituted myoglobins. J Biol Inorg Chem 10 11-24... [Pg.149]

Roncone R, Monzani E, Murtas M et al (2004) Engineering peroxidase activity in myoglobin the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine. Biochem J 377 717-724... [Pg.149]

Roncone R, Monzani E, Nicolis S, Casella L (2004) Engineering and prosthetic-group modification of myoglobin peroxidase activity, chemical stability and unfolding properties. Eur J Inorg Chem 2203-2213... [Pg.150]

The ferriheme protein metmyoglobin (metMb) at the physiological pH 7.4 was reported to bind the NO molecule reversibly yielding the nitrosyl adduct [metMb(NO)] the kinetics of the association and dissociation processes were investigated and a limiting dissociation mechanism was proposed (58,68). 2-His-l-Glu nonheme iron center engineered into myoglobin was reported capable to bind Fe(II) and reduce NO to N2O (69). [Pg.307]

The 2-His-l-Glu metal center commonly foimd in natimal nonheme iron enz5unes was engineered into myoglobin, and this new protein appears capable of binding not only Fe(II) but also Cu(I), and the sites are active in reducing NO to N2O via different intermediates (69). [Pg.312]

Ozaki SI, Roach MP, Matsui T, Watanabe Y (2001) Investigations of the roles of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin. Acc Chem Res 34 818-825... [Pg.154]

Molecular engineering of myoglobin The improvement of oxidation activity by replacing Phe-43 with tryptophan. Biochemistry 40, 1044-1052. [Pg.180]

Sigman, J.A., H.K. Kim, X. Zhao, J.R. Carey, and Y. Lu (2(X)3). The role of copper and protons in heme-copper oxidases Kinetic study of an engineered heme-copper center in myoglobin. Proc. Natl Acad Sci. USA 100, 3629-3634. [Pg.37]


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See also in sourсe #XX -- [ Pg.169 ]




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