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本文引用的文献

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Stereochemistry of iron in deoxyhaemoglobin.
Nature. 1982 Feb 11;295(5849):535-8. doi: 10.1038/295535a0.
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Nitrogenase from nifV mutants of Klebsiella pneumoniae contains an altered form of the iron-molybdenum cofactor.肺炎克雷伯氏菌nifV突变体的固氮酶含有一种铁钼辅因子的变体形式。
Biochem J. 1984 Jan 1;217(1):317-21. doi: 10.1042/bj2170317.
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Purification and characterization of the inactive MoFe protein (NifB-Kp1) of the nitrogenase from nifB mutants of Klebsiella pneumoniae.肺炎克雷伯氏菌nifB突变体固氮酶无活性钼铁蛋白(NifB-Kp1)的纯化与表征
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Nitrogenase XII. Mössbauer studies of the MoFe protein from Clostridium pasteurianum W5.固氮酶十二。巴氏梭菌W5钼铁蛋白的穆斯堡尔谱研究。
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The vanadium-iron protein of vanadium nitrogenase from Azotobacter chroococcum contains an iron-vanadium cofactor.来自褐球固氮菌的钒固氮酶的钒铁蛋白含有一个铁钒辅因子。
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Nitrogenase XI: Mössbauer studies on the cofactor centers of the MoFe protein from Azotobacter vinelandii OP.固氮酶XI:对棕色固氮菌OP菌株钼铁蛋白辅因子中心的穆斯堡尔谱研究
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Isolation of thiomolybdate compounds from the molybdenum-iron protein of clostridial nitrogenase.从梭菌固氮酶的钼铁蛋白中分离硫代钼酸盐化合物。
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肺炎克雷伯菌固氮酶铁钼辅因子的铁 K 边 X 射线吸收光谱

Iron K-edge X-ray absorption spectroscopy of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae.

作者信息

Arber J M, Flood A C, Garner C D, Gormal C A, Hasnain S S, Smith B E

机构信息

Department of Chemistry, University of Manchester, U.K.

出版信息

Biochem J. 1988 Jun 1;252(2):421-5. doi: 10.1042/bj2520421.

DOI:10.1042/bj2520421
PMID:3046607
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1149162/
Abstract

Iron K-edge X-ray absorption data for the iron-molybdenum cofactor ('FeMoco') from Klebsiella pneumoniae reported here provide the first evidence for long-range structural order in the cofactor [Fe...Fe(Mo) = 0.368 nm in addition to Fe...S = 0.22 nm and Fe...Fe(Mo) = 0.27 nm] and, in contrast with previously published data [Antonio, Teo, Orme-Johnson, Nelson, Groh, Lindahl, Kauzlarich & Averill (1982) J. Am. Chem. Soc. 104, 4703-4705], indicate that most of the iron centres are not co-ordinated to light (oxygen, nitrogen) atoms. This demonstrates that presently available chemical models for FeMoco are inadequate.

摘要

本文报道的肺炎克雷伯氏菌铁钼辅因子(“FeMoco”)的铁K边X射线吸收数据首次证明了该辅因子中存在长程结构有序性[除了铁硫键长为0.22纳米和铁铁(钼)键长为0.27纳米外,铁铁(钼)键长为0.368纳米],并且与之前发表的数据[安东尼奥、特奥、奥姆-约翰逊、尼尔森、格罗、林达尔、考兹拉里奇和埃弗里尔(1982年)《美国化学会志》104,4703 - 4705]相反,表明大多数铁中心并未与轻(氧、氮)原子配位。这表明目前可用的FeMoco化学模型并不充分。