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Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.
Proc Natl Acad Sci U S A. 1979 Oct;76(10):4986-9. doi: 10.1073/pnas.76.10.4986.
2
Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP. Nature of the iron centers.
Biochim Biophys Acta. 1978 Dec 20;537(2):185-207. doi: 10.1016/0005-2795(78)90504-4.
3
Iron-sulfur clusters in the molybdenum-iron protein component of nitrogenase. Electron paramagnetic resonance of the carbon monoxide inhibited state.
Biochemistry. 1979 Oct 30;18(22):4860-9. doi: 10.1021/bi00589a014.
4
Characterization of the iron-sulfur centers in succinate dehydrogenase.
Proc Natl Acad Sci U S A. 1979 Aug;76(8):3805-8. doi: 10.1073/pnas.76.8.3805.
5
Fluorine-19 chemical shifts as structural probes of metal-sulfur clusters and the cofactor of nitrogenase.
Proc Natl Acad Sci U S A. 1982 Nov;79(22):7056-60. doi: 10.1073/pnas.79.22.7056.
6
The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster.
J Biol Chem. 1979 Jun 25;254(12):4967-9.
7
Nitrogenase. VIII. Mössbauer and EPR spectroscopy. The MoFe protein component from Azotobacter vinelandii OP.
Biochim Biophys Acta. 1975 Jul 21;400(1):32-53. doi: 10.1016/0005-2795(75)90124-5.
8
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum.
J Mol Biol. 1998 Jul 24;280(4):669-85. doi: 10.1006/jmbi.1998.1898.
9
Nitrogenase: properties of the catalytically inactive complex between the Azotobacter vinelandii MoFe protein and the Clostridium pasteurianum Fe protein.
Biochim Biophys Acta. 1978 Dec 8;527(2):359-69. doi: 10.1016/0005-2744(78)90350-9.
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Metal and sulfur composition of iron-molybdenum cofactor of nitrogenase.
Proc Natl Acad Sci U S A. 1983 Jan;80(1):147-50. doi: 10.1073/pnas.80.1.147.
引用本文的文献
1
Structural Enzymology of Nitrogenase Enzymes.
Chem Rev. 2020 Jun 24;120(12):4969-5004. doi: 10.1021/acs.chemrev.0c00067. Epub 2020 Jun 15.
2
Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.
Proc Natl Acad Sci U S A. 1987 Oct;84(20):7066-9. doi: 10.1073/pnas.84.20.7066.
3
The unusual metal clusters of nitrogenase: structural features revealed by x-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum.
Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):1078-82. doi: 10.1073/pnas.90.3.1078.
4
A Mössbauer spectroscopic investigation of the redox behaviour of the molybdenum-iron protein from Klebsiella pneumoniae nitrogenase. Mechanistic and structural implications.
Biochem J. 1980 Nov 1;191(2):449-55. doi: 10.1042/bj1910449.
5
Fluorine-19 chemical shifts as structural probes of metal-sulfur clusters and the cofactor of nitrogenase.
Proc Natl Acad Sci U S A. 1982 Nov;79(22):7056-60. doi: 10.1073/pnas.79.22.7056.
6
Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii.
Proc Natl Acad Sci U S A. 1982 Jan;79(2):378-80. doi: 10.1073/pnas.79.2.378.
7
Low-temperature magnetic-circular-dichroism spectroscopy of the iron-molybdenum cofactor and the complementary cofactor-less MoFe protein of Klebsiella pneumoniae nitrogenase.
Biochem J. 1984 Apr 15;219(2):495-503. doi: 10.1042/bj2190495.
8
Nitrogenase from Klebsiella pneumoniae. An e.p.r. signal observed during enzyme turnover under ethylene is associated with the iron-molybdenum cofactor.
Biochem J. 1983 May 1;211(2):495-7. doi: 10.1042/bj2110495.
9
Evidence on intramolecular electron transfer in the MoFe protein of nitrogenase from Klebsiella pneumoniae from rapid-freeze electron-paramagnetic-resonance studies of its oxidation by ferricyanide.
Biochem J. 1983 Jan 1;209(1):207-13. doi: 10.1042/bj2090207.
10
Site-directed mutagenesis of the Klebsiella pneumoniae nitrogenase. Effects of modifying conserved cysteine residues in the alpha- and beta-subunits.
Biochem J. 1989 Nov 15;264(1):257-64. doi: 10.1042/bj2640257.
本文引用的文献
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Structure of the molybdoferredoxin complex from Clostridium pasteurianum and isolation of its subunits.
J Bacteriol. 1973 Feb;113(2):884-90. doi: 10.1128/jb.113.2.884-890.1973.
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Evidence for a catalytic-centre heterogeneity of molybdoferredoxin from Clostridium pasteurianum.
Eur J Biochem. 1973 Jun 15;35(3):401-9. doi: 10.1111/j.1432-1033.1973.tb02852.x.
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Synthetic analogs of the active sites of iron-sulfur proteins; X. Kinetics and mechanism of the ligand substitution reactions of arylthiols with the tetranuclear clusters [Fe4S4(SR)4]2 minus;
J Am Chem Soc. 1975 Feb 5;97(3):528-33. doi: 10.1021/ja00836a011.
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Letter: Extrusion of Fe2S2 and Fe4S4 cores from the active sites of ferredoxin proteins.
J Am Chem Soc. 1975 Jan 22;97(2):463-4. doi: 10.1021/ja00835a064.
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The molecular weight of, and evidence for two types of subunits in, the molybdenum-iron protein of Azotobacter vinelandii nitrogenase.
Biochem J. 1977 Jun 1;163(3):427-32. doi: 10.1042/bj1630427.
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Quantitative extrusions of the Fe4S4 cores of the active sites of ferredoxins and the hydrogenase of Clostridium pasteurianum.
J Am Chem Soc. 1977 Jan 19;99(2):584-95. doi: 10.1021/ja00444a044.
7
Nitrogenase XI: Mössbauer studies on the cofactor centers of the MoFe protein from Azotobacter vinelandii OP.
Biochim Biophys Acta. 1979 Jan 25;576(1):192-203. doi: 10.1016/0005-2795(79)90497-5.
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Isolation and partial characterization of two different subunits from the molybdenum-iron protein of Azotobacter vinelandii nitrogenase.
J Biol Chem. 1978 May 25;253(10):3422-6.
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The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster.
J Biol Chem. 1979 Jun 25;254(12):4967-9.
10
Isolation of an iron-molybdenum cofactor from nitrogenase.
Proc Natl Acad Sci U S A. 1977 Aug;74(8):3249-53. doi: 10.1073/pnas.74.8.3249.
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