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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 and insights are starting to be provided into the structures of the FeMo- co biosynthetic intermediates and into the biochemical details of Fe Mo-co synthesis. Expand
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, and it is a major contributor to the nitrogen cycle. Expand
Regulation of biological nitrogen fixation.
The paradigms of nitrogenase function, transcriptional control and post-translational regulation, as well as the variations on these schemes, described in various nitrogen-fixing bacteria are described. Expand
Functional characterization of three GlnB homologs in the photosynthetic bacterium Rhodospirillum rubrum: roles in sensing ammonium and energy status.
Surprisingly, in their regulation of the DRAT/DRAG system, GlnB and GlnJ appeared to be responsive not only to changes in nitrogen status but also toChanges in energy status, revealing a new role for this family of regulators in central metabolic regulation. Expand
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
In vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Purification and characterization of NifB cofactor, the product of NIFB protein.
NifB-co has been purified to homogeneity by a unique one-step method and is stable to repeated freeze-thaw cycles and is also stable in N-methylformamide, the solvent used for the isolation of FeMo-co. Expand
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
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
This x-ray structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems. Expand
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 and it is posit that cooH and cooFS are not cotranscribed. Expand
Mutagenesis and functional characterization of the glnB, glnA, and nifA genes from the photosynthetic bacterium Rhodospirillum rubrum.
The characterization of glnB, glnA, and nifA mutants and studies of their relationship to the regulation of nitrogen fixation are reported and the modification of glutamine synthetase appears to be similar to that seen in wild type. Expand