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Identification and characterization of functional homologs of nitrogenase cofactor biosynthesis protein NifB from methanogens. | LitMetric

Identification and characterization of functional homologs of nitrogenase cofactor biosynthesis protein NifB from methanogens.

Proc Natl Acad Sci U S A

Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900

Published: December 2015

AI Article Synopsis

  • NifB is a key protein that helps insert carbide into the M cluster of nitrogenase, critical for nitrogen fixation in *Azotobacter vinelandii*.
  • Researchers have identified two truncated versions of NifB from *Methanosarcina acetivorans* and *Methanobacterium thermoautotrophicum*, which lack a specific domain but still have unique SAM-binding capabilities.
  • These homologs can convert clusters in the presence of SAM and catalyze reactions leading to the incorporation of methyl-derived carbide into the M cluster, expanding the understanding of metallocluster assembly and methyltransferase function.*

Article Abstract

Nitrogenase biosynthesis protein NifB catalyzes the radical S-adenosyl-L-methionine (SAM)-dependent insertion of carbide into the M cluster, the cofactor of the molybdenum nitrogenase from Azotobacter vinelandii. Here, we report the identification and characterization of two naturally "truncated" homologs of NifB from Methanosarcina acetivorans (NifB(Ma)) and Methanobacterium thermoautotrophicum (NifB(Mt)), which contain a SAM-binding domain at the N terminus but lack a domain toward the C terminus that shares homology with NifX, an accessory protein in M cluster biosynthesis. NifB(Ma) and NifB(Mt) are monomeric proteins containing a SAM-binding [Fe4S4] cluster (designated the SAM cluster) and a [Fe4S4]-like cluster pair (designated the K cluster) that can be processed into an [Fe8S9] precursor to the M cluster (designated the L cluster). Further, the K clusters in NifB(Ma) and NifB(Mt) can be converted to L clusters upon addition of SAM, which corresponds to their ability to heterologously donate L clusters to the biosynthetic machinery of A. vinelandii for further maturation into the M clusters. Perhaps even more excitingly, NifB(Ma) and NifB(Mt) can catalyze the removal of methyl group from SAM and the abstraction of hydrogen from this methyl group by 5'-deoxyadenosyl radical that initiates the radical-based incorporation of methyl-derived carbide into the M cluster. The successful identification of NifB(Ma) and NifB(Mt) as functional homologs of NifB not only enabled classification of a new subset of radical SAM methyltransferases that specialize in complex metallocluster assembly, but also provided a new tool for further characterization of the distinctive, NifB-catalyzed methyl transfer and conversion to an iron-bound carbide.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4672821PMC
http://dx.doi.org/10.1073/pnas.1510409112DOI Listing

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