دورية أكاديمية
Design of silk proteins with increased heme binding capacity and fabrication of silk-heme materials.
| العنوان: | Design of silk proteins with increased heme binding capacity and fabrication of silk-heme materials. |
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| المؤلفون: | Rapson TD; CSIRO Black Mountain, Acton, ACT 2601, Australia., Liu JW; CSIRO Black Mountain, Acton, ACT 2601, Australia., Sriskantha A; CSIRO Black Mountain, Acton, ACT 2601, Australia., Musameh M; CSIRO, Clayton, Melbourne, VIC 3168, Australia., Dunn CJ; CSIRO, Clayton, Melbourne, VIC 3168, Australia., Church JS; CSIRO, Waurn Ponds, Geelong, VIC 3216, Australia., Woodhead A; CSIRO, Waurn Ponds, Geelong, VIC 3216, Australia., Warden AC; CSIRO Black Mountain, Acton, ACT 2601, Australia., Riley MJ; School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, QLD 4072, Australia., Harmer JR; Centre for Advanced Imaging, University of Queensland, St Lucia, QLD 4072, Australia., Noble CJ; Centre for Advanced Imaging, University of Queensland, St Lucia, QLD 4072, Australia., Sutherland TD; CSIRO Black Mountain, Acton, ACT 2601, Australia. Electronic address: Tara.Sutherland@CSIRO.au. |
| المصدر: | Journal of inorganic biochemistry [J Inorg Biochem] 2017 Dec; Vol. 177, pp. 219-227. Date of Electronic Publication: 2017 Sep 04. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 7905788 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3344 (Electronic) Linking ISSN: 01620134 NLM ISO Abbreviation: J Inorg Biochem Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: New York, Elsevier. |
| مواضيع طبية MeSH: | Protein Engineering*, Heme/*chemistry , Hemeproteins/*chemistry , Insect Proteins/*chemistry , Silk/*chemistry, Animals ; Bees ; Binding Sites ; Electromagnetic Phenomena ; Electron Spin Resonance Spectroscopy ; Histidine/chemistry ; Insect Proteins/genetics ; Mutation ; Protein Structure, Quaternary ; Silk/genetics |
| مستخلص: | In our previous studies, heme was bound into honeybee silk to generate materials that could function as nitric oxide sensors or as recoverable heterogeneous biocatalysts. In this study, we sought to increase the heme-binding capacity of the silk protein by firstly redesigning the heme binding site to contain histidine as the coordinating residue and secondly, by adding multiple histidine residues within the core of the coiled coil core region of the modified silk protein. We used detergent and a protein denaturant to confirm the importance of the helical structure of the silk for heme coordination. Aqueous methanol treatment, which was used to stabilize the materials, transformed the low-spin, six-coordinate heme to a five-coordinate high-spin complex, thus providing a vacant site for ligand binding. The optimal aqueous methanol treatment time that simultaneously maintains the helical protein structure and stabilizes the silk material without substantial leaching of heme from the system was determined. (Copyright © 2017 Elsevier Inc. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Coiled coil; De novo protein engineering; EPR; Heme; Honeybee silk; MCD |
| المشرفين على المادة: | 0 (Hemeproteins) 0 (Insect Proteins) 0 (Silk) 42VZT0U6YR (Heme) 4QD397987E (Histidine) |
| تواريخ الأحداث: | Date Created: 20171015 Date Completed: 20180710 Latest Revision: 20180710 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/j.jinorgbio.2017.08.031 |
| PMID: | 29031180 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1873-3344 |
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| DOI: | 10.1016/j.jinorgbio.2017.08.031 |