| Ab initio Studies on the Fe-S Protein Model Complexes |
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| 引用本文： | 张明瑜,于微舟,李晓天,江元生. Ab initio Studies on the Fe-S Protein Model Complexes[J]. 中国科学B辑(英文版), 1993, 0(6) |
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| 作者姓名： | 张明瑜 于微舟 李晓天 江元生 |
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| 作者单位： | Institute of Theoretical Chemistry，Jilin University，Changchun 130023，PRC，Institute of Theoretical Chemistry，Jilin University，Changchun 130023，PRC，Institute of Theoretical Chemistry，Jilin University，Changchun 130023，PRC，Chemistry Department of Nanjing University |
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| 基金项目： | Projiect supported by the National Natural Science Foundation of China |
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| 摘 要： | In this paper, ab initio calculations of the iron-sulfur protein model complexes have been completed on Fe_2S_2(SH)_2~(n-) and Fe_4S_4(SH)_4~(n-)(n=2, 3). The results indicate that the occupied terminal sulfur characteristic orbitals are found in the front orbital site and the energy levels of the occupied Fe 3d-like orbitals appear internally below the S-H bonding orbitals in the valence band. Although the energy sequence is different from what was reported in literature, our results are in agreement with the relevant experimental facts. We have discussed the reason that variations of the active sites are produced by various oxidation levels. The action mechanism of the Fe-S proteins as electron carriers in the biological processes is also explored preliminarily.
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| 关 键 词： | iron-sulfur protein αb initio calculation. |
Ab initio Studies on the Fe-S Protein Model Complexes |
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| ZHANG Ming-Yu YU Wei-Zhou LI Xiao-Tian JIANG Yuan-Sheng. Ab initio Studies on the Fe-S Protein Model Complexes[J]. Science in China(Chemistry), 1993, 0(6) |
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| Authors: | ZHANG Ming-Yu YU Wei-Zhou LI Xiao-Tian JIANG Yuan-Sheng |
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| Abstract: | In this paper, ab initio calculations of the iron-sulfur protein model complexes have been completed on Fe_2S_2(SH)_2~(n-) and Fe_4S_4(SH)_4~(n-)(n=2, 3). The results indicate that the occupied terminal sulfur characteristic orbitals are found in the front orbital site and the energy levels of the occupied Fe 3d-like orbitals appear internally below the S-H bonding orbitals in the valence band. Although the energy sequence is different from what was reported in literature, our results are in agreement with the relevant experimental facts. We have discussed the reason that variations of the active sites are produced by various oxidation levels. The action mechanism of the Fe-S proteins as electron carriers in the biological processes is also explored preliminarily. |
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