Bovine carbonyl lactoperoxidase structure at 2.0 Å resolution and infrared spectra as a function of pH
Yazarlar (10)
Amit K Singh
Michael L Smith
Shavait Yamini
Per-Ingvar Ohlsson
Mau Sinha
Punit Kaur
Sujata Sharma
Jan AK Paul
K-G Paul
| Makale Türü |
Özgün Makale
(Uluslararası alan indekslerindeki dergilerde yayınlanan tam makale)
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| Dergi Adı | The protein journal | ||
| Dergi ISSN | 1572-3887 | ||
| Makale Dili | – | Basım Tarihi | 01-2012 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 11-08-2012 |
| Cilt / Sayı / Sayfa | 31 / 7 / 598–608 | DOI | 10.1007/s10930-012-9436-3 |
| Makale Linki | https://link.springer.com/article/10.1007/s10930-012-9436-3 | ||
| UAK Araştırma Alanları |
Dedektör Teknolojisi
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| Özet |
| Lactoperoxidase (LPO) is a hemeprotein catalyzing the oxidation of thiocyanate and I− into antimicrobials and small aromatic organics after being itself oxidized by H2O2. LPO is excreted by the lungs, mammary glands, found in saliva and tears and protects mammals against bacterial, fungal and viral invasion. The Fe(II) form binds CO which inactivates LPO like many other hemeproteins. We present the 3-dimensional structure of CO–LPO at 2.0Å resolution and infrared (IR) spectra of the iron-bound CO stretch from pH 3 to 8.8 at 1 cm−1 resolution. The observed Fe–C–O bond angle of 132° is more acute than the electronically related Fe(III), CN–LPO with a Fe–C–N angle of 161°. The orientations of the two ligands are different with the oxygen of CO pointing towards the imidazole of distal His109 while the nitrogen of CN points away, the Fe(II) moves towards His109 while the Fe(III) moves away; both movements … |
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| Google Scholar | 25 |