Results 181 to 190 of about 33,406 (213)
Some of the next articles are maybe not open access.
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.
openaire +2 more sources
Nitrogenase Bioelectrocatalysis
ECS Meeting Abstracts, 2019Nitrogenase is the only enzyme capable of nitrogen reduction to ammonia. This talk will discuss cobaltocene and methyl viologen mediation schemes for MoFe and VFe nitrogenase, as well as strategies for nitrogenase bioelectrocatalysis in air. Bioelectrocatalysis of proton reduction, azide reduction, nitrite reduction, nitrogen reduction, and carbon ...
openaire +1 more source
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).
openaire +2 more sources
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).
openaire +2 more sources
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
openaire +2 more sources
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
openaire +3 more sources
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.
openaire +3 more sources
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.
openaire +3 more sources
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
openaire +2 more sources
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.
openaire +1 more source
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.
openaire +1 more source