scholarly journals Azotobacter vinelandii scaffold protein NifU transfers iron to NifQ as part of the iron-molybdenum cofactor biosynthesis pathway for nitrogenase

2021 ◽  
Author(s):  
Emma Barahona ◽  
Xi Jiang ◽  
Emilio Jiménez-Vicente ◽  
Luis M. Rubio ◽  
Manuel González-Guerrero
Keyword(s):  
Protein Interaction ◽  
Iron Content ◽  
Azotobacter Vinelandii ◽  
Biosynthesis Pathway ◽  
Biochemical Evidence ◽  
Protein Protein Interaction ◽  
Iron Sulfur ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis ◽  
Iron Molybdenum Cofactor

ABSTRACTAzotobacter vinelandii molybdenum-dependent nitrogenase obtains molybdenum from NifQ, a monomeric iron-sulfur molybdoprotein. This protein requires of a preexisting [Fe-S] cluster to form a [MoFe3S4] group to serve as specific donor during nitrogenase cofactor biosynthesis. Here, we show biochemical evidence for NifU being the donor of the [Fe-S] cluster. Protein-protein interaction studies using apo-NifQ and as-isolated NifU demonstrated the interaction between both proteins which is only effective when NifQ is unoccupied by its [Fe-S] cluster. The apo-NifQ iron content increased after the incubation with as-isolated NifU, reaching similar levels to holo-NifQ after the interaction between apo-NifQ and NifU with reconstituted transient [Fe4-S4] groups. These results also indicate the necessity of co-expressing NifU together with NifQ in the pathway to provide molybdenum for the biosynthesis of nitrogenase in engineered nitrogen-fixing plants.

scholarly journals Inhibition of Iron-Molybdenum Cofactor Biosynthesis by L127Δ NifH and Evidence for a Complex Formation between L127Δ NifH and NifNE

1999 ◽  
Vol 274 (41) ◽  
pp. 29413-29419 ◽  
Author(s):  
Priya Rangaraj ◽  
Matthew J. Ryle ◽  
William N. Lanzilotta ◽  
Paul J. Goodwin ◽  
Dennis R. Dean ◽  
...  
Keyword(s):  
Complex Formation ◽  
Molybdenum Cofactor ◽  
Cofactor Biosynthesis ◽  
Molybdenum Cofactor Biosynthesis ◽  
Iron Molybdenum Cofactor

scholarly journals Iron–Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein–Protein Interaction

2015 ◽  
Vol 33 (3) ◽  
pp. 643-656 ◽  
Author(s):  
Wojciech Delewski ◽  
Bogumiła Paterkiewicz ◽  
Mateusz Manicki ◽  
Brenda Schilke ◽  
Bartłomiej Tomiczek ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Specific Protein ◽  
Mutational Robustness ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Protein Protein Interaction ◽  
Iron Sulfur

scholarly journals The First Step of Neurospora crassa Molybdenum Cofactor Biosynthesis: Regulatory Aspects under N-Derepressing and Nitrate-Inducing Conditions

2020 ◽  
Vol 8 (4) ◽  
pp. 534
Author(s):  
Simon Wajmann ◽  
Thomas W. Hercher ◽  
Sabine Buchmeier ◽  
Robert Hänsch ◽  
Ralf R. Mendel ◽  
...  
Keyword(s):  
Neurospora Crassa ◽  
Transcriptional Control ◽  
Molybdenum Cofactor ◽  
Transfer Reactions ◽  
Biosynthesis Pathway ◽  
Prosthetic Group ◽  
Regulatory Aspects ◽  
Cofactor Biosynthesis ◽  
Single Transcript ◽  
Molybdenum Cofactor Biosynthesis

Molybdenum cofactor (Moco) is the active site prosthetic group found in all Moco dependent enzymes, except for nitrogenase. Mo-enzymes are crucial for viability throughout all kingdoms of life as they catalyze a diverse set of two electron transfer reactions. The highly conserved Moco biosynthesis pathway consists of four different steps in which guanosine triphosphate is converted into cyclic pyranopterin monophosphate, molybdopterin (MPT), and subsequently adenylated MPT and Moco. Although the enzymes and mechanisms involved in these steps are well characterized, the regulation of eukaryotic Moco biosynthesis is not. Within this work, we described the regulation of Moco biosynthesis in the filamentous fungus Neurospora crassa, which revealed the first step of the multi-step pathway to be under transcriptional control. We found, that upon the induction of high cellular Moco demand a single transcript variant of the nit-7 gene is increasingly formed pointing towards, that essentially the encoded enzyme NIT7-A is the key player for Moco biosynthesis activity in Neurospora.

scholarly journals Protein networks in the maturation of human iron–sulfur proteins

Metallomics ◽  
2018 ◽  
Vol 10 (1) ◽  
pp. 49-72 ◽  
Author(s):  
Simone Ciofi-Baffoni ◽  
Veronica Nasta ◽  
Lucia Banci
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Networks ◽  
Interaction Networks ◽  
Protein Networks ◽  
Protein Protein Interaction ◽  
Iron Sulfur ◽  
Complex Process ◽  
Protein Protein Interaction Networks ◽  
Cellular Compartments ◽  
S Proteins

The maturation of human Fe–S proteins is a complex process involving protein–protein interaction networks distributed across different cellular compartments.

scholarly journals Characterization of MOCS1A, an Oxygen-sensitive Iron-Sulfur Protein Involved in Human Molybdenum Cofactor Biosynthesis

2004 ◽  
Vol 279 (33) ◽  
pp. 34721-34732 ◽  
Author(s):  
Petra Hänzelmann ◽  
Heather L. Hernández ◽  
Christian Menzel ◽  
Ricardo García-Serres ◽  
Boi Hanh Huynh ◽  
...  
Keyword(s):  
Molybdenum Cofactor ◽  
Iron Sulfur ◽  
Oxygen Sensitive ◽  
Cofactor Biosynthesis ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Molybdenum Cofactor Biosynthesis
Sign in / Sign up

Export Citation Format

Share Document