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通过高场脉冲电子顺磁共振光谱法研究的cd1亚硝酸还原酶的血红素d1亚硝酰配合物。

Heme d1 nitrosyl complex of cd1 nitrite reductase studied by high-field-pulse electron paramagnetic resonance spectroscopy.

作者信息

Radoul Marina, Centola Fabio, Rinaldo Serena, Cutruzzolà Francesca, Pecht Israel, Goldfarb Daniella

机构信息

Department of Chemical Physics, Weizmann Institute of Science, Rehovot 76100, Israel.

出版信息

Inorg Chem. 2009 May 4;48(9):3913-5. doi: 10.1021/ic802355y.

DOI:10.1021/ic802355y
PMID:19348457
Abstract

W-band (95 GHz) HYSCORE and pulse ENDOR are used to characterize the nitrosyl d(1) heme complex (d(1)NO) of cd(1) nitrite reductase from Pseudomonas aeruginosa in the wild type and the Y10F mutant. The spectra and the derived (14)N hyperfine and quadrupole interactions were found to be the same for wt and Y10F. This suggests that Tyr10 does not influence the NO ligand orientation in the reduced state in solution. This study is the first application of HYSCORE at high fields and shows its potential for characterizing low gamma nuclei with large hyperfine couplings.

摘要

采用W波段(95吉赫兹)的高分辨脉冲电子自旋回波包络调制谱(HYSCORE)和脉冲电子核双共振(ENDOR)技术,对野生型和Y10F突变型铜绿假单胞菌中亚硝酸还原酶的亚硝酰基d(1)血红素复合物(d(1)NO)进行了表征。结果发现,野生型和Y10F突变型的谱图以及由此得到的(14)N超精细和四极相互作用是相同的。这表明,在溶液中还原态下,酪氨酸10(Tyr10)并不影响NO配体的取向。本研究是高场HYSCORE技术的首次应用,展示了其在表征具有大超精细耦合的低γ核方面的潜力。

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Heme d1 nitrosyl complex of cd1 nitrite reductase studied by high-field-pulse electron paramagnetic resonance spectroscopy.通过高场脉冲电子顺磁共振光谱法研究的cd1亚硝酸还原酶的血红素d1亚硝酰配合物。
Inorg Chem. 2009 May 4;48(9):3913-5. doi: 10.1021/ic802355y.
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Two enzymes with a common function but different heme ligands in the forms as isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha.两种具有共同功能但分离形式下血红素配体不同的酶。来自施氏假单胞菌和嗜泛硫菌的亚硝酸还原酶细胞色素cd1氧化形式中血红素基团的光学和磁性性质。
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Solvent accessibility in the distal heme pocket of the nitrosyl d(1)-heme complex of Pseudomonas stutzeri cd(1) nitrite reductase.假单胞菌 d(1)-heme 亚硝酸盐还原酶中硝酰基 d(1)-heme 复合物远端 heme 口袋的溶剂可及性。
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The functional role of the structure of the dioxo-isobacteriochlorin in the catalytic site of cytochrome cd for the reduction of nitrite.二氧代异菌绿素结构在细胞色素cd催化位点用于亚硝酸盐还原中的功能作用。
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