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Biosynthesis of the iron-molybdenum cofactor of nitrogenase.
The iron-molybdenum cofactor (FeMo-co), located at the active site of the molybdenum nitrogenase, is one of the most complex metal cofactors known to date. During the past several years, an intensiveExpand
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Maturation of nitrogenase: a biochemical puzzle.
The nitrogenase enzyme catalyzes the reductive breakage of the very strong triple bond of N2 to generate NH3 in a process known as biological nitrogen fixation. Biological nitrogen fixation is anExpand
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Functional characterization of three GlnB homologs in the photosynthetic bacterium Rhodospirillum rubrum: roles in sensing ammonium and energy status.
The GlnB (P(II)) protein, the product of glnB, has been characterized previously in the photosynthetic bacterium Rhodospirillum rubrum. Here we describe identification of two other P(II) homologs inExpand
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Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli.
The hybrid cluster protein (HCP; formerly termed the prismane protein) has been extensively studied due to its unique spectroscopic properties. Although the structural and spectroscopicExpand
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In vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Purification and characterization of NifB cofactor, the product of NIFB protein.
The requirement of NIFB activity for the biosynthesis of iron-molybdenum cofactor (FeMo-co) can be satisfied by the addition of the low molecular weight product of NIFB, termed NifB cofactorExpand
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Regulation of biological nitrogen fixation.
Biological nitrogen fixation, a process found only in some prokaryotes, is catalyzed by the nitrogenase enzyme complex. Bacteria containing nitrogenase occupy an indispensable ecological niche,Expand
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Carbon monoxide-dependent growth of Rhodospirillum rubrum.
Under dark, anaerobic conditions in the presence of sufficient nickel, Rhodospirillum rubrum grows with a doubling time of under 5 h by coupling the oxidation of CO to the reduction of H+ to H2.Expand
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Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum has been determined to 2.8-Å resolution. The CODH family, for which the R. rubrum enzymeExpand
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Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii.
Rnf proteins are proposed to form membrane-protein complexes involved in the reduction of target proteins such as the transcriptional regulator SoxR or the dinitrogenase reductase component ofExpand
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Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system.
A 3.7-kb DNA region encoding part of the Rhodospirillum rubrum CO oxidation (coo) system was identified by using oligonucleotide probes. Sequence analysis of the cloned region indicated four completeExpand
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