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Iron-only Fe-nitrogenase underscores common catalytic principles in biological nitrogen fixation
Nature Catalysis, 2023Christian Trncik +2 more
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1977
The biochemistry of nitrogenase has been reviewed so frequently in the past few years that the production of a comprehensive review at this point seems unwarranted. My colleagues and I have published two lengthy reviews in which most of the recent developments have been analyzed (Orme-Johnson and Davis, 1977; Orme-Johnson et al., 1977).
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The biochemistry of nitrogenase has been reviewed so frequently in the past few years that the production of a comprehensive review at this point seems unwarranted. My colleagues and I have published two lengthy reviews in which most of the recent developments have been analyzed (Orme-Johnson and Davis, 1977; Orme-Johnson et al., 1977).
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Nitrogenases without molybdenum
Trends in Biochemical Sciences, 1989For 50 years molybdenum had been considered to have an indispensable catalytic function for nitrogen fixation. Two nitrogenases recently isolated from the bacterium Azotobacter have changed this view. One is a vanadium-containing enzyme and the other lacks both molybdenum and vanadium. Similar nitrogenases may occur in other nitrogen-fixing organisms.
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Catalysis and structure of nitrogenases
Current Opinion in Structural Biology, 2023In providing bioavailable nitrogen as building blocks for all classes of biomacromolecules, biological nitrogen fixation is an essential process for all organismic life. Only a single enzyme, nitrogenase, performs this task at ambient conditions and with ATP as an energy source.
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Biosynthesis of the Metalloclusters of Nitrogenases
Annual Review of Biochemistry, 2016Nitrogenase is a versatile metalloenzyme that is capable of catalyzing two important reactions under ambient conditions: the reduction of nitrogen (N2) to ammonia (NH3), a key step in the global nitrogen cycle; and the reduction of carbon monoxide (CO) and carbon dioxide (CO2) to hydrocarbons, two reactions useful for recycling carbon waste into ...
Markus W. Ribbe, Yilin Hu
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The Critical E4 State of Nitrogenase Catalysis.
Biochemistry, 2018The reaction catalyzed by the nitrogenase enzyme involves breaking the stable triple bond of the dinitrogen molecule and is consequently considered among the most challenging reactions in biology.
M. Rohde +4 more
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Purification of Nitrogenase Proteins
2011Nitrogenase is one of the most complex enzymes known to date. The extensively studied molybdenum nitrogenase consists of two protein components and three metal centers that are critical for nitrogenase activity. The inherent complexity of this enzyme system, which is further compounded by the sensitivity of the metal clusters toward oxygen, makes the ...
Jared A. Wiig +4 more
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Assembly of Nitrogenase MoFe Protein
Biochemistry, 2008Assembly of nitrogenase MoFe protein is arguably one of the most complex processes in the field of bioinorganic chemistry, requiring, at least, the participation of nifS, nifU, nifB, nifE, nifN, nifV, nifQ, nifZ, nifH, nifD, and nifK gene products. Previous genetic studies have identified factors involved in MoFe protein assembly; however, the exact ...
Aaron W. Fay +4 more
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Purification of Nitrogenase Proteins
2018A major hurdle in the studies of nitrogenase, one of the most complicated metalloenzymes known to date, is to obtain large amounts of intact, active proteins. Nitrogenase and related proteins are often multimeric and consist of metal centers that are critical for their activities.
Chi-Chung, Lee +2 more
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