Fluorescence lifetime analysis of nitrite reductase from Alcaligenes xylosoxidans at the single-molecule level reveals the enzyme mechanism.
作者信息
Tabares Leandro C, Kostrz Dorota, Elmalk Abdalmohsen, Andreoni Alessio, Dennison Christopher, Aartsma Thijs J, Canters Gerard W
机构信息
Leiden Institute of Physics, Huygens Laboratory, Leiden University, Niels Bohrweg 2, 2333CA Leiden, The Netherlands.
出版信息
Chemistry. 2011 Oct 17;17(43):12015-9. doi: 10.1002/chem.201102063. Epub 2011 Sep 16.
PMID:21922585
Abstract
摘要
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Fluorescence lifetime analysis of nitrite reductase from Alcaligenes xylosoxidans at the single-molecule level reveals the enzyme mechanism.木糖氧化产碱杆菌亚硝酸还原酶在单分子水平的荧光寿命分析揭示了酶的作用机制。
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Nitrite reductase from Achromobacter xylosoxidans forms stable trimers in dilute solution.
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Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 A resolution: comparison of blue and green nitrite reductases.木糖氧化产碱杆菌GIFU 1051蓝色亚硝酸还原酶在2.05埃分辨率下的1型铜结构：蓝色和绿色亚硝酸还原酶的比较
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Evidence for two distinct azurins in Alcaligenes xylosoxidans (NCIMB 11015): potential electron donors to nitrite reductase.木糖氧化产碱杆菌（NCIMB 11015）中两种不同天青蛋白的证据：亚硝酸盐还原酶的潜在电子供体。
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X-ray scattering using synchrotron radiation shows nitrite reductase from Achromobacter xylosoxidans to be a trimer in solution.利用同步辐射进行的X射线散射显示，木糖氧化无色杆菌中的亚硝酸还原酶在溶液中是三聚体。
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The subunit structure of nitrite reductase purified from the denitrifier Achromobacter cycloclastes.
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Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism.木糖氧化产碱杆菌亚硝酸还原酶的Met144Ala、Asp92Asn和His254Phe突变体的生化及晶体学研究为酶作用机制提供了深入见解。
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