Article
Microbiology
Xi Jiang, Diana Coroian, Emma Barahona, Carlos Echavarri-Erasun, Rocio Castellanos-Rueda, Alvaro Eseverri, Jose A. Aznar-Moreno, Stefan Buren, Luis M. Rubio
Summary: Biological nitrogen fixation is the process of converting inert atmospheric nitrogen gas into reactive ammonia, which can reduce the dependency on nitrogen fertilizers in plants by introducing functional nitrogenase. NifB is a critical protein in nitrogen fixation and can be restored by expressing nifB genes from different sources. Accumulation of functional NifB proteins in chloroplasts and mitochondria is crucial for engineering biological nitrogen fixation in plants.
Article
Biochemistry & Molecular Biology
Yiling A. Liu, Robert Quechol, Joseph B. Solomon, Chi Chung Lee, Markus W. Ribbe, Yilin Hu, Britt Hedman, Keith O. Hodgson
Summary: This review focuses on the recent work that sheds light on the role of NifB in the formation of the [Fe8S9C] core of the nitrogenase cofactor, highlighting the structure, function, and mechanism of this unique radical SAM methyltransferase.
JOURNAL OF INORGANIC BIOCHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Ana Perez-Gonzalez, Emilio Jimenez-Vicente, Alvaro Salinero-Lanzarote, Derek F. Harris, Lance C. Seefeldt, Dennis R. Dean
Summary: Azotobacter vinelandii produces three genetically distinct nitrogenase isozymes, among which Fe-only nitrogenase has lower catalytic activity for N-2 fixation and is only produced when Mo and V are not available.
MOLECULAR MICROBIOLOGY
(2022)
Article
Chemistry, Inorganic & Nuclear
William R. Buratto, Ricardo B. Ferreira, Vincent J. Catalano, Ricardo Garcia-Serres, Leslie J. Murray
Summary: In this study, reactions between triiron complexes and sulfido or bromide complexes led to redistribution of ligands and electrons, resulting in the formation of mixed-ligand multiiron complexes. The cleavage and redistribution observed in these complexes resemble the necessary Fe-S bond cleavage for substrate activation in nitrogenase enzymes, offering a new perspective on the lability of Fe-S bonds in FeS clusters.
DALTON TRANSACTIONS
(2021)
Article
Biochemical Research Methods
Wenshu He, Stefan Buren, Can Baysal, Xi Jiang, Teresa Capell, Paul Christou, Luis M. Rubio
Summary: The engineering of nitrogen fixation in plants requires the assembly of an active prokaryotic nitrogenase complex. However, the production of NifB protein in plants is challenging due to its insolubility and sensitivity to oxygen. In this study, transgenic rice plants expressing NifB from Archaea were generated, and the NifB proteins accumulated as soluble proteins in planta. The purified proteins were also functional in the in vitro synthesis assay. This study represents a significant step towards the biosynthesis of a functional NifDK complex for biological nitrogen fixation in cereals.
ACS SYNTHETIC BIOLOGY
(2022)
Article
Biotechnology & Applied Microbiology
Gema Lopez-Torrejon, Stefan Buren, Marcel Veldhuizen, Luis M. Rubio
Summary: Engineering nitrogenase in eukaryotes is challenging due to its genetic complexity and oxygen sensitivity, but the Fe-only nitrogenase can serve as a simple model. By expressing stable Fe-only nitrogenase component proteins in the low-oxygen mitochondria matrix of S. cerevisiae, it was shown to be active even in low oxygen conditions.
MICROBIAL BIOTECHNOLOGY
(2021)
Article
Multidisciplinary Sciences
Michael Rohde, Konstantin Laun, Ingo Zebger, Sven T. Stripp, Oliver Einsle
Summary: In addition to its role in biological nitrogen fixation, vanadium-containing nitrogenase is also capable of reducing carbon monoxide to hydrocarbons. The protein exhibits a specific ligand binding site that suggests a mechanistic route for CO reduction and hydrocarbon formation.
Review
Microbiology
Rhys Grinter, Chris Greening
Summary: F-420 is a redox cofactor produced by many bacteria and archaea, structurally similar to FAD and FMN but catalytically similar to NAD and NADP. Understanding of its distribution, biosynthesis, role, and applications has progressed significantly in the past 5 years. New evidence suggests F-420 is synthesized across bacterial and archaeal domains through horizontal and vertical gene transfer, with new biosynthetic pathways and processes being discovered.
FEMS MICROBIOLOGY REVIEWS
(2021)
Article
Biochemistry & Molecular Biology
Christian Trncik, Tanja Mueller, Philipp Franke, Oliver Einsle
Summary: This study presents the crystal structure of the ADP-bound reductase component AnfH of the iron-only nitrogenase and compares it with other iron protein homologs. The results show that all three iron proteins adopt the same conformation. Cross-reactivity assays reveal that AnfH is compatible with iron-only nitrogenase and to a lesser degree with the vanadium-containing enzyme, but not with molybdenum nitrogenase.
JOURNAL OF INORGANIC BIOCHEMISTRY
(2022)
Article
Chemistry, Multidisciplinary
Chang Yuan, Wan-Ting Jin, Zhao-Hui Zhou
Summary: By comparing N-2 and CO bound FeMo-cofactors, we have calculated the oxidation states of the iron and molybdenum atoms in FeMo-cos. We found that different coordination modes and binding sites can affect the distribution of oxidation states.
NEW JOURNAL OF CHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Kresimir Rupnik, Lee Rettberg, Kazuki Tanifuji, Johannes G. Rebelein, Markus W. Ribbe, Yilin Hu, Brian J. Hales
Summary: NifB, a radical SAM enzyme, is involved in the biosynthesis of the L cluster and contains the characteristic motifs associated with SAM binding. The study of NifB reveals the mechanism of L cluster biosynthesis through interaction with SAM.
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
(2021)
Article
Chemistry, Inorganic & Nuclear
Benjamin S. Mitchell, Andrei Chirila, Kevin J. Anderton, Werner Kaminsky, Alexandra Velian
Summary: This study provides insights into the electronic structure of the Fe/Co6Se8 cluster and the redox cooperativity between the Fe active site and the Co6Se8 support. Different types of oxidized Fe/Co6Se8 clusters are isolated depending on the counterion used, and experimental characterization and computational analysis are used to investigate the charge distribution. The findings show that the charge is shared between the Fe edge site and the Co6Se8 core upon oxidation.
INORGANIC CHEMISTRY
(2023)
Article
Chemistry, Multidisciplinary
Alex McSkimming, Daniel L. M. Suess
Summary: The study demonstrates that embedding an [MoFe3S4] cluster in a protective ligand environment allows for N-2 binding at Fe; further substitution induces charge transfer, generating Fe-N multiple-bond character; covalent interactions within the cluster play a critical role in N-2 binding and activation.
Article
Agronomy
Vatsala Koul, Mandira Kochar
Summary: The small RNA sSp_p6 from Azospirillum brasilense Sp245 plays an important role in nitrogen metabolism, being modulated under carbon and nitrogen stress and interacting with nitrogen fixation-related genes, showing its essential role in biological nitrogen fixation. Furthermore, overexpression of sSp_p6 can increase lateral root formation in the host plant Sorghum, leading to improved plant root morphology.
Article
Chemistry, Multidisciplinary
Alexandra C. Brown, Daniel L. M. Suess
Summary: Attempts to generate open coordination sites for N2 binding at synthetic Fe-S clusters often result in cluster oligomerization. However, recent studies have shown that oligomerization reactions can be prevented by using sterically protective supporting ligands in Mo-Fe-S clusters, enabling N2 complex formation. This strategy has now been extended to Fe-only Fe-S clusters. Evaluation: 7 out of 10.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Multidisciplinary Sciences
Wonchull Kang, Chi Chung Lee, Andrew J. Jasniewski, Markus W. Ribbe, Yilin Hu
Article
Chemistry, Multidisciplinary
Wonchull Kang, Lee A. Rettberg, Martin T. Stiebritz, Andrew J. Jasniewski, Kazuki Tanifuji, Chi Chung Lee, Markus W. Ribbe, Yilin Hu
Summary: NifB is a crucial radical SAM enzyme for nitrogenase cofactor assembly, and the X-ray crystal structures of MtNifB reveal insights into the mechanism of cofactor biosynthesis. The coordinated binding of SAM in holo MtNifB suggests important pathways for SAM cleavage and cofactor core formation.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Article
Biochemistry & Molecular Biology
Jasper Liedtke, Chi Chung Lee, Kazuki Tanifuji, Andrew J. Jasniewski, Markus W. Ribbe, Yilin Hu
Summary: This study presents a biochemical and spectroscopic characterization of a Mo-nitrogenase variant with a citrate-substituted cofactor analogue, revealing the impact of citrate substitution on CO and N2 reduction pathways. The results suggest a crucial role of homocitrate in substrate reduction by nitrogenase and the potential to modulate product profiles of nitrogenase reactions through organic ligand substitution.
Article
Chemistry, Multidisciplinary
Kelsey R. Miller, Saborni Biswas, Andrew Jasniewski, Alec H. Follmer, Ankita Biswas, Therese Albert, Sinan Sabuncu, Emile L. Bominaar, Michael P. Hendrich, Pierre Moenne-Loccoz, A. S. Borovik
Summary: The research focuses on designing artificial proteins to achieve active sites with entatic states by simulating a controlled environment. Utilizing biotin-streptavidin technology, artificial di-Fe cores containing Fe centers have been successfully assembled, revealing the process of Fe center separation regulation by the protein host.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Editorial Material
Multidisciplinary Sciences
Wonchull Kang, Chi Chung Lee, Andrew J. jasniewski, Markus W. Ribbe, Yilin Hu
Summary: Peters and colleagues' claim of contradicting our findings on the dynamic structure of the nitrogenase metallocofactor during N-2 reduction is refuted by our biochemical and structural data, which conclusively demonstrate the binding of dinitrogen species to the nitrogenase cofactor.
Article
Biochemistry & Molecular Biology
Kresimir Rupnik, Lee Rettberg, Kazuki Tanifuji, Johannes G. Rebelein, Markus W. Ribbe, Yilin Hu, Brian J. Hales
Summary: NifB, a radical SAM enzyme, is involved in the biosynthesis of the L cluster and contains the characteristic motifs associated with SAM binding. The study of NifB reveals the mechanism of L cluster biosynthesis through interaction with SAM.
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Shahid Shahid, Mahbbat Ali, Desiree Legaspi-Humiston, Jarett Wilcoxen, A. Andrew Pacheco
Summary: The decaheme enzyme cytochrome c nitrite reductase facilitates the reduction of nitrite to ammonium with different kinetics of intermediate formation when strong or weak reductants are used, indicating its complex mechanism influenced by the catalyst.
Article
Chemistry, Multidisciplinary
Kazuki Tanifuji, Andrew J. Jasniewski, David Villarreal, Martin T. Stiebritz, Chi Chung Lee, Jarett Wilcoxen, Yasuhiro Okhi, Ruchira Chatterjee, Isabel Bogacz, Junko Yano, Jan Kern, Britt Hedman, Keith O. Hodgson, R. David Britt, Yilin Hu, Markus W. Ribbe
Summary: The study investigates the insertion of the 'ninth sulfur' in the biosynthesis of cofactors, revealing its role in cluster transfer and the incorporation of Se2- and Te2- species into the cluster. The research also proposes a mechanism involving the reduction of SO32- to S2- for labeling the catalytically important belt region for nitrogenase mechanistic investigations.
Article
Chemistry, Physical
Chi Chung Lee, Wonchull Kang, Andrew J. Jasniewski, Martin T. Stiebritz, Kazuki Tanifuji, Markus W. Ribbe, Yilin Hu
Summary: This study provides direct evidence that N2 is captured on the M-cluster via electron and sulfur depletion, and the N2-captured state is catalytically active in generating NH3. The study also reveals the conditions for product release and the dynamic changes of belt-sulfurs during catalysis. These findings highlight the crucial role of the mobilization of cofactor belt-sulfurs in the nitrogenase reaction.
Review
Chemistry, Multidisciplinary
Sven T. Stripp, Benjamin R. Duffus, Vincent Fourmond, Christophe Leger, Silke Leimkueshler, Shun Hirota, Yilin Hu, Andrew Jasniewski, Hideaki Ogata, Markus W. Ribbe
Summary: Gases like H-2, N-2, CO2, and CO are important feedstock for green energy conversion and as sources of nitrogen and carbon. However, their industrial transformation and production require significant energy input, whereas nature efficiently converts them at ambient conditions using gas-processing metalloenzymes (GPMs). In this review, the importance of the cofactor/protein interface in GPMs is emphasized, and the effects of second and outer coordination sphere on catalytic activity are discussed.
Article
Chemistry, Multidisciplinary
Joseph B. Solomon, Mahtab F. Rasekh, Caleb J. Hiller, Chi Chung Lee, Kazuki Tanifuji, Markus W. Ribbe, Yilin Hu
Summary: The Fe proteins MaNifH and MaVnfH from Methanosarcina acetivorans exhibit different reactivities towards C1 substrates in the all-ferrous state, with MaVnfH showing weaker reactivity due to adopting the all-ferrous state at a more positive reduction potential. This suggests the possibility of MaVnfH accessing the all-ferrous state under physiological conditions, which has implications for the reaction mechanism of nitrogenase.