Results 151 to 160 of about 6,680 (190)
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Nitrogenase: standing at the crossroads
Current Opinion in Chemical Biology, 2000Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia, which is central to the process of biological nitrogen fixation. Recent progress towards establishing the mechanism of action of this complex metalloenzyme reflects the contributions of a combination of structural, biochemical, spectroscopic, synthetic and theoretical ...
Rees, Douglas C., Howard, James B.
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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 ...
Yilin, Hu, Markus W, Ribbe
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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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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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Cluster assembly in nitrogenase
Essays in Biochemistry, 2017The versatile enzyme system nitrogenase accomplishes the challenging reduction of N2and other substrates through the use of two main metalloclusters. For molybdenum nitrogenase, the catalytic component NifDK contains the [Fe8S7]-core P-cluster and a [MoFe7S9C-homocitrate] cofactor called the M-cluster.
Nathaniel S, Sickerman +4 more
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Nature Microbiology, 2018
An alternative nitrogenase enzyme that only utilizes iron as its cofactor is shown to reduce carbon dioxide while actively fixing dinitrogen, so that it simultaneously produces ammonium, hydrogen and methane.
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An alternative nitrogenase enzyme that only utilizes iron as its cofactor is shown to reduce carbon dioxide while actively fixing dinitrogen, so that it simultaneously produces ammonium, hydrogen and methane.
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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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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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