PMID:8631723

Citation	Davis, R, Lehman, L, Petrovich, R, Shah, VK, Roberts, GP and Ludden, PW (1996) Purification and characterization of the alternative nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum. J. Bacteriol. 178:1445-50
Abstract	The alternative nitrogenase from a nifH mutant of the photosynthetic bacterium Rhodospirillum rubrum has been purified and characterized. The dinitrogenase protein (ANF1) contains three subunits in an apparent alpha2beta2gamma2 structure and contains Fe but no Mo or V. A factor capable of activating apo-dinitrogenase (lacking the FeMo cofactor) from Azotobacter vinelandii was extracted from the alternative dinitrogenase protein with N-methylformamide. The electron paramagnetic resonance (EPR) signal of the dinitrogenase protein is not characteristic of the EPR signals of molybdenum- or vanadium-containing dinitrogenases. The alternative dinitrogenase reductase (ANF2) was purified as an alpha2 dimer containing an Fe4S4 cluster and exhibited an EPR spectrum characteristic of dinitrogenase reductases. The enzyme complex reduces protons to H2 very well but reduces N2 to ammonium poorly. Acetylene is reduced to a mixture of ethylene and ethane.
Links	PubMed PMC177820
Keywords	Acetylene/metabolism; Apoenzymes/chemistry; Apoenzymes/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Dinitrogenase Reductase/chemistry; Dinitrogenase Reductase/metabolism; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Ethane/metabolism; Iron/analysis; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/metabolism; Isoenzymes/chemistry; Isoenzymes/metabolism; Metals/analysis; Mutation; Nitrogenase/chemistry; Nitrogenase/genetics; Nitrogenase/metabolism; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Quaternary Ammonium Compounds/metabolism; Rhodospirillum rubrum/enzymology; Rhodospirillum rubrum/genetics; Substrate Specificity; Tricarboxylic Acids/analysis
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
RHORU:NIFH	part_of	GO:0016610: nitrogenase complex	ECO:0000315: mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
RHORU:NIFH		GO:0016610: nitrogenase complex	ECO:0000315:		C		Figure 3	complete CACAO 3383

References

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