Binding of dinitrogen to an iron–sulfur–carbon site

Čorić, Ilija; Mercado, Brandon Q.; Bill, Eckhard; Vinyard, David J.; Holland, Patrick L.

doi:10.1038/nature15246

Cited by 239 publications

(137 citation statements)

References 35 publications

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“…In the 13 C NMR spectrum ( Figure S4, SI section), a total of 22 signals are evidenced, consistent with the structure of 3. Among the most representative ones are the carbonyl C-atom at 165.7 ppm, and the imidazole-based C4 and C5 at 132.3 ppm.…”

Section: The Synthesis Of Nn'-bis(2-[n''n''-dimethyl-s-thiocarbamoymentioning

confidence: 56%

“…All other reagents were obtained from commercial suppliers unless otherwise stated; 2-formyl-4-methyl-6-[3,5-bis(trifluoromethyl) phenyl]-N,N-dimethyl-S-phenylthiocarbamate (A) was prepared as previously described. 20 1 H, 13 C, and 19 F nuclear magnetic resonance (NMR) spectra were recorded with a JEOL Eclipse 300 spectrometer at 300, 75, and 282 MHz, respectively, using the residual protiated solvent signal or tetramethylsilane (TMS) as internal references (TMS d = 0.00, CHCl 3 d = 7.26 ppm). Electron ionization mass spectrometry (EI-MS) experiments were performed with a JEOL JMS-AX505HA spectrometer.…”

Section: Methodsmentioning

confidence: 99%

“…Among the most representative ones are the carbonyl C-atom at 165.7 ppm, and the imidazole-based C4 and C5 at 132.3 ppm. 13 C DEPT-135 helped the assignment, with the negative phase signal at 52.0 ppm arising from the methylene bridge between the imidazole and arylthiocarbamate groups; the two signals centered around 37.2 correspond to the N-methyl groups, and the signal at 21.2 to the aromatic para-methyl C-atom ( Figure S5, SI section). The aromatic signals cannot be assigned unequivocally with the available data.…”

Section: The Synthesis Of Nn'-bis(2-[n''n''-dimethyl-s-thiocarbamoymentioning

confidence: 99%

“…The bulky groups offer steric protection to prevent the formation of oligomeric or polymeric iron complexes with bridging thiolates. While there are several examples of iron complexes that activate dinitrogen with B, N, C, and P-based ligands, [14][15][16][17][18][19] the example reported by Holland and co-workers 13 is the only one reported to date that has atoms of sulfur and carbon as coordination sites for the metallic center at the same time. Inspired by the SCS (sulfur-carbon-sulfur) pincer ligand, we undertook the synthesis of the NHC ligand with bulky sulfur-containing groups that is herein reported.…”

Section: Introductionmentioning

confidence: 99%

“…Among the potential applications of ligands with bulky substituents, the synthesis of biologically inspired metal complexes that activate small molecules such as CO 2 and N 2 in an analogous fashion to metalloenzymatic active sites is one of the most successfully exploited. As an iconic example of these transformations inspired by the active site of metalloenzymes, Holland and co-workers 13 developed iron complexes that feature a dithiolate ligand, which provides the metal ions with sulfur and carbon-based donors. This donor set, analogous to that present in the active site of nitrogenase, appears to be necessary for the activation of the N 2 ; the sulfur atoms are provided by two chelating arylthiolate donors with 2,4,6-triisopropylphenyl substituents in the ortho position of the thiolates.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Silver Complex of an N-Heterocyclic Carbene Ligand with Bulky Thiocarbamate Groups

Robles‐Marín¹,

Mondragón²,

Flores-Álamo³

et al. 2018

J. Braz. Chem. Soc.

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Section: The Synthesis Of Nn'-bis(2-[n''n''-dimethyl-s-thiocarbamoymentioning

confidence: 56%

Section: Methodsmentioning

confidence: 99%

Section: The Synthesis Of Nn'-bis(2-[n''n''-dimethyl-s-thiocarbamoymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Silver Complex of an N-Heterocyclic Carbene Ligand with Bulky Thiocarbamate Groups

Robles‐Marín¹,

Mondragón²,

Flores-Álamo³

et al. 2018

J. Braz. Chem. Soc.

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Nitrogenase: Metal Cluster Models

Ohta

2019

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Nitrogenases are metalloenzymes that are involved in the biological fixation of nitrogen. Nitrogenases contain the following metal–sulfur clusters: the [Fe 4 S 4 ] cluster, the P‐cluster, and one of the FeMo‐cofactor, the FeV‐cofactor, or the FeFe‐cofactor. At present, structures of all clusters except for that of the FeFe‐cofactor have been determined by X‐ray diffraction studies of nitrogenases. The metal–sulfur clusters in nitrogenases have remained challenging synthetic targets due to their unique structural features. In addition, the elucidation of the properties of the cluster models, including their structural, spectroscopic, magnetic, and electronic characteristics, as well as their reactivity may further our understanding of the properties and functionality of nitrogenases. This article reviews hitherto reported structural models of nitrogenase metalloclusters. Although the synthesis of reliable structural models of the FeMo‐cofactor and the FeV‐cofactor remains challenging, high‐precision structural models have already been obtained for the [Fe 4 S 4 ] cluster and the P‐cluster, which has allowed systematic investigations into their structures and redox properties. This article also summarizes the current state‐of‐the‐art regarding the functional modeling of nitrogenases with metal–sulfur clusters, which includes the reduction of hydrazine to ammonia and of C 1 ‐substrates to hydrocarbons, and N 2 ‐binding. Moreover, the reactivity of nitrogenase with a structural model inserted instead of the FeMo‐cofactor has recently been reported.

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Assembly of Nitrogenase FeMoco and P Cluster

Sickerman

Rettberg

et al. 2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

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The catalytic reduction of dinitrogen by nitrogenase metalloenzymes to form ammonia is a critically important process in the global nitrogen cycle. Accomplishing this difficult reduction reaction under ambient conditions requires the cooperation of a series of nitrogenase proteins. The three main nitrogenase variants known are the iron/molybdenum‐containing Mo‐nitrogenase, the iron/vanadium‐containing V‐nitrogenase, and the iron‐only nitrogenase. All three variants utilize a MgATP‐dependent reductase component and perform substrate reduction within a larger catalytic component. In the case of Mo‐nitrogenase (encoded by nif genes), the reductase component, NifH, contains a canonical [Fe 4 S 4 ] cluster; the catalytic component, NifDK, contains two unique metal‐containing clusters that are necessary for N 2 reduction: the site of catalytic substrate reduction, the [MoFe 7 S 9 C( R ‐homocitrate)] FeMo cofactor, also called M cluster, and a capacitor‐like [Fe 8 S 7 ]‐core unit called the P cluster. Biosynthesis of these two sophisticated metalloclusters involves the concerted effort of several nitrogenase assembly proteins. For both clusters, simple 2Fe units are first converted to [Fe 4 S 4 ] clusters on the scaffold protein NifU with assistance by the cysteine desulfurase enzyme NifS. For M‐cluster biosynthesis, the 4Fe building blocks are supplied to the scaffold protein NifB to equip this radical S ‐adenosylmethionine (SAM) enzyme with a SAM‐responsive cluster and a pair of 4Fe units called the “K cluster”. One equivalent of SAM donates a methyl group to the K cluster on NifB, while a second equivalent of SAM abstracts a hydrogen atom from the transferred methyl group. The S –CH 2 ⋅ species formed by the second SAM equivalent facilitates cluster fusion, and following concomitant addition of a “9th sulfur” atom and deprotonation of the methylene unit, the [Fe 8 S 9 C]‐core L cluster is generated. The L cluster is handed off from NifB to another scaffold protein NifEN for further processing. On NifEN, the precursor cluster is matured to the M cluster through the actions of NifH, inserting homocitrate and a reduced form of Mo to produce completed M cluster. Following a conformational rearrangement, NifEN directly transfers the M cluster to a high‐affinity site on NifDK, which embeds the cofactor within the catalytic active site. P cluster biosynthesis begins on NifDK with a pair of protein subunit‐bridging 4Fe clusters termed the P* cluster. Through the actions of NifH and assistance by the chaperone‐like protein NifZ, reductive coupling of the clusters occurs to form functional P cluster. Genetic deletion mutants of NifDK suggest that P‐cluster maturation occurs in a stepwise manner and that M‐cluster insertion is only possible after P‐cluster assembly. This chapter outlines the complex facets of Mo‐nitrogenase metallocluster biosynthesis.

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Binding of dinitrogen to an iron–sulfur–carbon site

Cited by 239 publications

References 35 publications

Silver Complex of an N-Heterocyclic Carbene Ligand with Bulky Thiocarbamate Groups

Silver Complex of an N-Heterocyclic Carbene Ligand with Bulky Thiocarbamate Groups

Nitrogenase: Metal Cluster Models

Assembly of Nitrogenase FeMoco and P Cluster

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