Results 231 to 240 of about 47,392 (275)
Some of the next articles are maybe not open access.
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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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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Crystallization of Nitrogenase Proteins
2018Nitrogenase is the only known enzymatic system capable of reducing atmospheric dinitrogen to ammonia. This unique reaction requires tightly choreographed interactions between the nitrogenase component proteins, the molybdenum-iron (MoFe)- and iron (Fe)-proteins, as well as regulation of electron transfer between multiple metal centers that are only ...
Wenke, Belinda B. +2 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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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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Advances in inorganic biochemistry, 1990
Recently, it has been demonstrated that both A. vinelandii and A. chroococcum have the ability to synthesize several different nitrogen-fixing enzymes. Both species can produce a Mo- or V-containing nitrogenase while A. vinelandii can also generate an all-Fe form of the enzyme.
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Recently, it has been demonstrated that both A. vinelandii and A. chroococcum have the ability to synthesize several different nitrogen-fixing enzymes. Both species can produce a Mo- or V-containing nitrogenase while A. vinelandii can also generate an all-Fe form of the enzyme.
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2014
Abstract Nitrogenases are a family of metalloenzymes that catalyse a key step in the global nitrogen cycle: the adenosine triphosphate (ATP)-dependent reduction of dinitrogen (N2) to ammonia (NH3). The molybdenum (Mo)-nitrogenase is the best characterised member of this enzyme family.
Wiig, J. +2 more
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Abstract Nitrogenases are a family of metalloenzymes that catalyse a key step in the global nitrogen cycle: the adenosine triphosphate (ATP)-dependent reduction of dinitrogen (N2) to ammonia (NH3). The molybdenum (Mo)-nitrogenase is the best characterised member of this enzyme family.
Wiig, J. +2 more
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Light-driven dinitrogen reduction catalyzed by a CdS:nitrogenase MoFe protein biohybrid
Science, 2016K. Brown +10 more
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