EC Number   |
General Information |
Reference |
|---|
    1.18.6.1 | evolution |
NifEN and MoFe protein have evolved from the replication and divergence of a common ancestral gene. NifEN is catalytically active early on in the course of evolution, when the mantle of earth is likely more reduced. Later, NifEN might have gradually evolved into an effective enzyme with a wide range of substrates, i.e. the MoFe protein, while in the meantime adjusting its own role toward synthesizing a catalytically more powerful cofactor, i.e. the iron-molybdenum cofactor |
714796 |
| 1.18.6.1 | evolution |
substrate specificity and evolutionary implications of a recombinant chimeric NifDK enzyme carrying NifB-co at its active site, NifDK/NifB-co, overview |
-, 715017 |
| 1.18.6.1 | evolution |
the ability of V nitrogenase to catalyze both CO and N2 reductions suggests a potential link between the evolution of carbon and nitrogen cycles |
716922 |
| 1.18.6.1 | metabolism |
NifB and NifEN are two essential elements immediately adjacent to each other along the biosynthetic pathway of FeMoco. The 8Fe-precursor is present in the NifEN entity of a synthetic NifEN-B fusion protein, and additional [Fe4S4]-type cluster species are present in the NifB entity of NifEN-B. The cluster species in NifEN-B consist of both SAM-motif- and non-SAM-motif-bound [Fe4S4]-type clusters. The non-SAM-motif [Fe4S4]-cluster is a NifB-bound intermediate of FeMoco assembly, which could be converted to the 8Fe-precursor in a SAM-dependent mechanism |
728672 |
| 1.18.6.1 | metabolism |
posttranslational regulation of nitrogenase activity in Rhodopseudomonas palustris depends on proteins DraT2, an ADP-ribosyltransferase, and GlnK2, an NtrC-regulated PII protein. GlnK2 is not well expressed in ammonium-grown NifA mutant cells that express nitrogenase genes constitutively and produce H2 when grown with ammonium as a nitrogen source. The mutant strain has elevated nitrogenase activity due to overexpression of the nif genes, and this increased amount of expression overwhelms a basal level of activity of DraT2 in ammonium-grown cells. Insufficient levels of both GlnK2 and DraT2 allow H2 production by an nifA* mutant grown with ammonium. Inactivation of the nitrogenase posttranslational modification system by mutation of draT2 results in increased H2 production by the ammonium-grown mutant cells |
721351 |
| 1.18.6.1 | more |
comparison of reaction mecanisms of nitrogenase, EC 1.18.6.1, and multiheme cytochrome c nitrite reductase, ccNIR, EC 1.7.2.2, overview |
742740 |
| 1.18.6.1 | more |
like the nif-encoded molybdenum nitrogenase, the vnf-encoded V nitrogenase is composed of a specific reductant and a catalytic component. Both nitrogenases use a catalytic mechanism that involves ATP-dependent electron transfer from a reductant, the nifH- or vnfH-encoded Fe protein, to the catalytic component, i.e. nifDK-encoded MoFe protein or vnfDGK-encoded VFe protein, and the reduction of N2 at the cofactor site, i.e. FeMoco or FeVco, of the latter |
716922 |
| 1.18.6.1 | more |
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum, FeMo, cofactor. It is an alpha2beta2 tetramer that is homologous to the catalytic MoFe protein, NifDK, component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK, NifEN crystal structure analysis, overview |
716924 |
| 1.18.6.1 | more |
nitrogenase consists of the Fe protein, encoded by nifH, and the MoFe protein, encoded by nifD and nifK. The Fe protein is a homodimer containing a single [4Fe-4S] cluster and functions as an ATP-dependent electron donor to the MoFe protein, which is bound at the active site and alpha2beta2 heterotetramer with each nifD-encoded alpha subunit coordinating the FeMo cofactor that binds and reduces substrate, while alpha plus the nifK-encoded beta subunits coordinate the [8Fe-7S] P-cluster |
-, 713837 |
| 1.18.6.1 | more |
nitrogenase is a protein complex that is required for biological nitrogen fixation. It is made up of a nitrogenase, which is a NifD2/NifK2 heterotetramer, and a nitrogenase reductase, which is a homodimer of NifH |
713656 |
