Active Site Variants of Myoglobin

With the development of bacterial expression systems for Mb described earlier and with the known diversity of metal coordination 

Comparison of the heme environments at the active sites of horse heart myoglobin 40) and yeast cytochrome c peroxidase 41). 

Introduction of tbiolate ligation at position 93 has also been reported (69, 70, 73). Again subtle species-specific differences in sequence on the proximal side of the heme binding pocket result in significant differences in behavior between closely related proteins. In this case, the spectroscopic properties of the human H93C variant (69, 70) were consistent with the presence of five-coordinate, cysteine-coordinated high-spin Fe(III). On the other hand, similar studies of the corresponding 

---

Cloning and Expression of Recombinant Myoglobin Active Site Variants of Myoglobin... 

---