| Autor: |
Yosca TH; Department of Chemistry, Pennsylvania State University , University Park, State College, Pennsylvania 16802, United States., Behan RK, Krest CM, Onderko EL, Langston MC, Green MT |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of the American Chemical Society [J Am Chem Soc] 2014 Jun 25; Vol. 136 (25), pp. 9124-31. Date of Electronic Publication: 2014 Jun 13. |
| DOI: |
10.1021/ja503588n |
| Abstrakt: |
To provide insight into the iron(IV)hydroxide pK(a) of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9-9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies. We find no indication of ferryl protonation over this pH range, allowing us to set an upper limit of 2.7 on the iron(IV)hydroxide pK(a) in myoglobin. Together with the recent determination of an iron(IV)hydroxide pK(a) ∼ 12 in the thiolate-ligated heme enzyme cytochrome P450, this result provides insight into Nature's ability to tune catalytic function through its choice of axial ligand. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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