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Showing 1 to 3 of 3 for “"FeBMb"”.
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Characterizing a structural and functional model of nitric oxide reductase performing NO and O2 reduction in engineered myoglobin
… was introduced near the heme of CuBMb, called FeBMb. Crystallographic and/or spectroscopic studies showed that FeBMb could bind Fe or Cu in its engineered FeB site, and was observed to be both a structural and functional model of native NORs through multiple generations of mutants6,7 Still …
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Engineering Myoglobin Into Both a Structural and Functional Model of Nitric Oxide Reductase
To date, FeBMb is the first protein model of the FeB site of NOR and provides the first evidence, from an NOR model, that the identity of the metal in analogous non-heme metal binding sites of HCO (i.e., CuB) and NOR (i.e., FeB) can tune NO activity. In summary, FeBMb is both a structural and …
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Understanding structure-function relations in heme-copper oxidase using myoglobin-based enzyme models
… an alternate, we have used a myoglobin mutant (FeBMb) that not only possesses a heme-nonheme metal center similar to HCOs, but can also bind copper, iron and their redox-inactive analogue zinc at its nonheme metal center. Oxygen reduction enzymatic assays reveal that Fe-FeBMb and Cu-FeBMb …