期刊論文
| 學年 | 89 |
|---|---|
| 學期 | 2 |
| 出版（發表）日期 | 2001-07-01 |
| 作品名稱 | Protein-coenzyme Interactions in adenosylcobalamin-dependent glutamate mutase |
| 作品名稱（其他語言） | |
| 著者 | Huhta, M.S.; Chen, H.P.; Hemann, C.; Hille, C.R.; Marsh, E.N. |
| 單位 | 淡江大學化學學系 |
| 出版者 | London: Portland Press |
| 著錄名稱、卷期、頁數 | Biochemical Journal 355(1), pp.131-137 |
| 摘要 | Glutamate mutase catalyses an unusual isomerization involving free-radical intermediates that are generated by homolysis of the cobalt-carbon bond of the coenzyme adenosylcobalamin (coenzyme B(12)). A variety of techniques have been used to examine the interaction between the protein and adenosylcobalamin, and between the protein and the products of coenzyme homolysis, cob(II)alamin and 5'-deoxyadenosine. These include equilibrium gel filtration, isothermal titration calorimetry, and resonance Raman, UV-visible and EPR spectroscopies. The thermodynamics of adenosylcobalamin binding to the protein have been examined and appear to be entirely entropy-driven, with DeltaS=109 J.mol(-1).K(-1). The cobalt-carbon bond stretching frequency is unchanged upon coenzyme binding to the protein, arguing against a ground-state destabilization of the cobalt-carbon bond of adenosylcobalamin by the protein. However, reconstitution of the enzyme with cob(II)alamin and 5'-deoxyadenosine, the two stable intermediates formed subsequent to homolysis, results in the blue-shifting of two of the bands comprising the UV-visible spectrum of the corrin ring. The most plausible interpretation of this result is that an interaction between the protein, 5'-deoxyadenosine and cob(II)alamin introduces a distortion into the ring corrin that perturbs its electronic properties. |
| 關鍵字 | Enzyme;Resonance Raman spectroscopy;Vitamin B 12 |
| 語言 | en |
| ISSN | 0264-6021 |
| 期刊性質 | 國外 |
| 收錄於 | |
| 產學合作 | |
| 通訊作者 | |
| 審稿制度 | |
| 國別 | GBR |
| 公開徵稿 | |
| 出版型式 | 紙本 |
| 相關連結 |
機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/61695 ) |