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• W2076352189 abstract "Nitrogenase activity in the photosynthetic bacterium Rhodospirillum rubrum is reversibly regulated by ADP‐ribosylation of a specific arginine residue of dinitrogenase reductase based on the cellular nitrogen or energy status. In this paper, we have investigated the ability of nicotinamide adenine dinucleotide, NAD (the physiological ADP‐ribose donor), and its analogs to support covalent modification of dinitrogenase reductase in vitro. R. rubrum dinitrogenase reductase can be modified by DRAT in the presence of 2 mM NAD, but not with 2 mM nicotinamide mononucleotide (NMN) or nicotinamide adenine dinucleotide phosphate (NADP). We also found that the apo‐ and the all‐ferrous forms of R. rubrum dinitrogenase reductase are not substrates for covalent modification. In contrast, Azotobacter vinelandii dinitrogenase reductase can be modified by the dinitrogenase reductase ADP‐ribosyl transferase (DRAT) in vitro in the presence of either 2 mM NAD, NMN or NADP as nucleotide donors. We found that: (1) a simple ribose sugar in the modification site of the A. vinelandii dinitrogenase reductase is sufficient to inactivate the enzyme, (2) phosphoADP‐ribose is the modifying unit in the NADP‐modified enzyme, and (3) the NMN‐modified enzyme carries two ribose‐phosphate units in one modification site. This is the first report of NADP‐ or NMN‐dependent modification of a target protein by an ADP‐ribosyl transferase." @default.
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• W2076352189 date "2005-10-05" @default.
• W2076352189 modified "2023-10-18" @default.
• W2076352189 title "NAD-, NMN-, and NADP-dependent modification of dinitrogenase reductases from<i>Rhodospirillum rubrum</i>and<i>Azotobacter vinelandii</i>" @default.
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• W2076352189 doi "https://doi.org/10.1016/j.febslet.2005.09.057" @default.
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