| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1925257 | Archives of Biochemistry and Biophysics | 2014 | 8 Pages |
•Structural factors influencing the O2 affinities of DHP and SW Mb have been examined.•The distal His Nε–heme iron distance increase is correlated with decreased O2 affinity.•The increased DHP function is previously attributed to longer distal His–heme iron distance.•The rotated proximal His in DHP may be important to compensate the decreased O2 affinity.•DHP has evolved its heme environment to gain significantly enhanced peroxidase capability.
Sea worm, Amphitrite ornata, has evolved its globin (an O2 carrier) also to serves as a dehaloperoxidase (DHP) to detoxify haloaromatic pollutants generated by competing species. A previous mutagenesis study by our groups on both DHP and sperm whale myoglobin (SW Mb) revealed some structural factors that influence the dehaloperoxidase activities (significantly lower for Mb) of both proteins. Using an isocyanide/O2 partition constant measurement method in this study, we have examined the effects of these structural factors on the O2 equilibrium constants (KO2) of DHP, SW Mb, and their mutants. A clear trend of decreasing O2 affinity and increasing catalytic activity along with the increase in the distal His Nε–heme iron distance is observed. An H93K/T95H Mb double mutant mimicking the DHP proximal His positioning exhibited markedly enhanced O2 affinity, confirming the essential effect of proximal His rotation on the globin function of DHP. For DHP, the L100F, T56G and M86E variants showed the effects of distal volume, distal His flexibility and proximal electronic push, respectively, on the O2 affinity. This study provides insights into how DHP has evolved its heme environment to gain significantly enhanced peroxidase capability without compromising its primary function as an O2 carrier.
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