Metallodithiolates as Ligands in Coordination, Bioinorganic, and Organometallic Chemistry

Denny, Jason A.; Darensbourg, Marcetta Y.

doi:10.1021/cr500659u

Cited by 130 publications

(130 citation statements)

References 198 publications

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“…In line with the pseudo-C 2v symmetry of the M(CO) 4 fragments, IR spectra of tetracarbonyls 7-10 in CH 2 Cl 2 solution feature four ν CO bands, the energies of which support a Ni II M 0 oxidation state formalism (Table 1 and Figure 2). The average ν CO energies of the Ni II W 0 complexes are ca.…”

Section: Resultsmentioning

confidence: 64%

“…Indeed, complexes of the type [Ni II L 2 (SR) 2 ] are versatile metalloligands with basicities comparable to that of 2,2Ј-bipyridine. [3] For example, Ni II diaminodithiolates have been incorporated into several multinuclear species, [4] including [N,NЈ-bis(2-sulfidoethyl)diazacyclooctane]NiM(CO) 4 (1: M = Mo; 2: M = W), [5] which features a topical NiS 2 M core ( Figure 1). Of comparable basicity are Ni II diphosphinodithiolates -these Figure 1.…”

Section: Introductionmentioning

confidence: 99%

“…also form stable Ni II Mo 0 species such as tetracarbonyl 3. [6] The present study makes use of the modularity with which one can prepare [L 2 Ni(SR) 2 M(CO) 4 ] complexes. Employed here are [Ni(dppe)(pdt)] [7] and [Ni(dcpe)(pdt)] [8] building blocks, which, while similar to the Ni II fragment in 3, retain some conformational flexibility when ligated to another metal.…”

Section: Introductionmentioning

confidence: 99%

“…[11] Described now are NiS 2 M (M = Mo, W) derivatives that blend hydrodesulfurization and hydrogenase themes into a promising catalytic motif. 4 ] (10) in good yields; heating is required in the latter two cases (Scheme 2). Robust and crystalline, the complexes are unaffected by air for short periods, although their solutions are more sensitive.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Nickel‐Molybdenum and Nickel‐Tungsten Dithiolates: Hybrid Models for Hydrogenases and Hydrodesulfurization

2015

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Section: Resultsmentioning

confidence: 64%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Nickel‐Molybdenum and Nickel‐Tungsten Dithiolates: Hybrid Models for Hydrogenases and Hydrodesulfurization

2015

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“…It is tempting to assume that the presence of strictly conserved Cys-X-Cys motifs in both AcsF Ch and ACS is not purely coincidental (37), but serves to have binding sites with similar affinity for Ni 2ϩ in both proteins. Once nickel is bound to the apoACS-AcsF Ch complex, MgATP is required to activate ACS.…”

Section: Nickelmentioning

confidence: 99%

AcsF Catalyzes the ATP-dependent Insertion of Nickel into the Ni,Ni-[4Fe4S] Cluster of Acetyl-CoA Synthase

Gregg

Goetzl

Jeoung

et al. 2016

Journal of Biological Chemistry

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Acetyl-CoA synthase (ACS) catalyzes the reversible condensation of CO, CoA, and a methyl-cation to form acetyl-CoA at a unique Ni,Ni-[4Fe4S] cluster (the A-cluster). However, it was unknown which proteins support the assembly of the A-cluster. We analyzed the product of a gene from the cluster containing the ACS gene, cooC2 from Carboxydothermus hydrogenoformans, named AcsF Ch , and showed that it acts as a maturation factor of ACS. AcsF Ch and inactive ACS form a stable 2:1 complex that binds two nickel ions with higher affinity than the individual components. The nickel-bound ACS-AcsF Ch complex remains inactive until MgATP is added, thereby converting inactive to active ACS. AcsF Ch is a MinD-type ATPase and belongs to the CooC protein family, which can be divided into homologous subgroups. We propose that proteins of one subgroup are responsible for assembling the Ni,Ni-[4Fe4S] cluster of ACS, whereas proteins of a second subgroup mature the [Ni4Fe4S] cluster of carbon monoxide dehydrogenases.The cellular maturation of metalloenzymes, previously considered a spontaneous process in vivo, typically depends on a machinery of uptake, storage, processing, and delivery factors (1). How metalloenzymes mature has been investigated for some systems, revealing surprisingly complex maturation pathways (2-8). Enzymes containing nickel, although still relatively small in number, play critical roles in archaea, bacteria, and eukarya, through which they impact the global hydrogen (Ni,Fe-hydrogenase), nitrogen (urease), and carbon (acetylCoA synthase, carbon monoxide dehydrogenase, and methylCoM reductase) cycles (9). For most of these enzymes, we now have a good understanding of how nickel is incorporated into the active site (8, 10).The nickel-enzymes acetyl-CoA synthase (ACS) 2 and carbon monoxide dehydrogenase (CODH) are found in a variety of anaerobic microbes, including bacterial sulfate reducers, acetogens, and hydrogenogens, as well as archaeal methanogens and sulfate reducers, where they act as the prime CO 2 and CO converter (11)(12)(13)(14). ACS and CODH can be found as independent monofunctional enzymes in Carboxydothermus hydrogenoformans (15) but are typically found in other microorganisms as protein complexes: in acetogens ACS and CODH form a bifunctional (␣␤) 2 complex, whereas in methanogens they are part of a large (␣␤␥␦⑀) 8 multienzyme complex (11,13,15,16). CODHs catalyze the reversible reduction of CO 2 to CO at the C-cluster, in which a single nickel ion, embedded within a 3Fe-4S scaffold with an additional iron in exo, binds and activates CO and CO 2 for turnover (17)(18)(19). ACS catalyzes the reversible condensation of CO, CoA, and a methyl-cation donated by the methylated corrinoid iron-sulfur protein to form acetyl-CoA (13). ACS depends on a Ni,Ni-[4Fe4S] cluster (also called A-cluster) for activity, in which the two nickel ions have distinct coordinations: the nickel ion distal to the [4Fe4S] cluster (Ni d ) is coordinated by two amide nitrogen atoms and two cysteine thiolates within a Cys-X-Cys ...

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Bioinspired and biomolecular catalysts for energy conversion and storage

Salamatian

Bren

2022

FEBS Letters

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Metalloenzymes are remarkable for facilitating challenging redox transformations with high efficiency and selectivity. In the area of alternative energy, scientists aim to capture these properties in bioinspired and engineered biomolecular catalysts for the efficient and fast production of fuels from low‐energy feedstocks such as water and carbon dioxide. In this short review, efforts to mimic biological catalysts for proton reduction and carbon dioxide reduction are highlighted. Two important recurring themes are the importance of the microenvironment of the catalyst active site and the key role of proton delivery to the active site in achieving desired reactivity. Perspectives on ongoing and future challenges are also provided.

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Metallodithiolates as Ligands in Coordination, Bioinorganic, and Organometallic Chemistry

Cited by 130 publications

References 198 publications

Nickel‐Molybdenum and Nickel‐Tungsten Dithiolates: Hybrid Models for Hydrogenases and Hydrodesulfurization

Nickel‐Molybdenum and Nickel‐Tungsten Dithiolates: Hybrid Models for Hydrogenases and Hydrodesulfurization

AcsF Catalyzes the ATP-dependent Insertion of Nickel into the Ni,Ni-[4Fe4S] Cluster of Acetyl-CoA Synthase

Bioinspired and biomolecular catalysts for energy conversion and storage

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