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Nature. 1992 Dec 10;360(6404):553-60. doi: 10.1038/360553a0 Q148.52025

Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from azotobacter vinelandii

来自氮源细菌的固氮酶钼铁蛋白的晶体结构及其功能含义 翻译改进

J Kim  1, D C Rees

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  • 1 Division of Chemistry and Chemical Engineering 147-75CH, California Institute of Technology, Pasadena, California 91125, USA.
  • DOI: 10.1038/360553a0 PMID: 25989647

    摘要 Ai翻译

    The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined at 2.7 Å resolution. The α- and β-subunits in this α (2) β (2) tetramer have similar polypeptide folds. The FeMo-cofactor is completely encompassed by the α-subunit, whereas the P-cluster pair occurs at the interface between α- and β-subunits. Structural similarities are apparent between nitrogenase and other electron transfer systems, ... ...点击完成人机验证后继续浏览
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    期刊名:Nature

    缩写:NATURE

    ISSN:0028-0836

    e-ISSN:1476-4687

    IF/分区:48.5/Q1

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    Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from azotobacter vinelandii