Synthesis and characterization of [S2MoS2Cu(n-SPhF)]2−(n=o, m, p) clusters: Potential 19F-NMR structural probes for Orange Protein

Maiti, Biplab K.; Avilés, Teresa; Moura, Isabel; Pauleta, Sofia R.; Moura, José J. G.

doi:10.1016/j.inoche.2014.04.006

Cited by 4 publications

(3 citation statements)

References 28 publications

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“…To overcome this, we have synthesized EPR or NMR active ORP metal derivatives by replacing the native copper ion with non-native metal ions like iron, cobalt, nickel, and cadmium ions, [15][16][17] or coordinating, at Cu-site, small organic thiol or fluorinated-thiol ligands ( 1 H or 19 F NMR) [15][16][17] (Figure 5). We attempted to reconstitute the apo-ORP with a synthesized semi-structural model compound with thiol derivatives, [15][16][17] but these model compounds have low solubility and stability in biological buffers. Therefore, suitable inorganic model compounds are required in order to recognize the cluster binding site.…”

Section: Orp Model Compoundsmentioning

confidence: 99%

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Molybdenum‐Copper Antagonism In Metalloenzymes And Anti‐Copper Therapy

Maiti,

Moura,

Moura

2024

ChemBioChem

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The connection between 3d (Cu) and 4d (Mo) via the “Mo‐S‐Cu” unit is called Mo‐Cu antagonism. Biology offers case studies of such interactions in metalloproteins such as Mo/Cu‐CO Dehydrogenases (Mo/Cu‐CODH), and Mo/Cu Orange Protein (Mo/Cu‐ORP). The CODH significantly maintains the CO level in the atmosphere below the toxic level by converting it to non‐toxic CO2 for respiring organisms. Several model studies were synthesized to understand the structure‐function relationship of these native enzymes. However, this interaction was first observed in ruminants, and they convert molybdate (MoO42–) into tetrathiomolybdate (MoS42–; TTM), reacting with cellular Cu to yield biological unavailable Mo/S/Cu cluster, then developing Cu‐deficiency diseases. These findings inspire the use of TTM as a Cu‐sequester drug, especially for treating Cu‐dependent human diseases such as Wilson diseases (WD) and cancer. It is well known that a balanced Cu homeostasis is essential for a wide range of biological processes, but negative consequence leads to cell toxicity. Therefore, this review aims to connect the Mo‐Cu antagonism in metalloproteins and anti‐copper therapy.

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Section: Orp Model Compoundsmentioning

confidence: 99%

“…The first inorganic model of ORP was reported by Maiti et al in 2004. [15] As both Mo and Cu are EPR silent and there is no suitable NMR reporter, more Mo/Cu derivatives were also synthesized as NMR and EPR probes [16][17][18][19] for finding the exact location in the protein cavity, but these probes failed to give fruitful results.…”

Section: Introductionmentioning

confidence: 99%

Molybdenum‐Copper Antagonism In Metalloenzymes And Anti‐Copper Therapy

Maiti,

Moura,

Moura

2024

ChemBioChem

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“…Therefore, the metal cofactor is manipulated by substituting the diamagnetic Cu I atom with paramagnetic or interesting NMR active metal reporters or coordinating the metal core with a small organic thiol ligand ( 1 H or 19 F NMR). In order to achieve our aims, we have reported a few synthetic inorganic semi-model compounds, where Mo-Cu cluster coordinated nonbiological thiols and fluorinated thiols are characterized by 1 H-NMR and 19 F-NMR respectively [153,154]. In addition, reconstitution of the NMR active cadmium atom into [S 2 MoS 2 CuS 2 MoS 2 ] 3− is originated a 113 Cd-NMR active compound, [S 2 MoS 2 CdS 2 MoS 2 ] 2− [153].…”

Section: Spectroscopic Probes Orpmentioning

confidence: 99%

Native Protein Template Assisted Synthesis of Non-Native Metal-Sulfur Clusters

Maiti

Moura

2022

BioChem

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Metalloenzymes are the most proficient nature catalysts that are responsible for diverse biochemical transformations introducing excellent selectivity and performing at high rates, using intricate mutual relationships between metal ions and proteins. Inspired by nature, chemists started using naturally occurring proteins as templates to harbor non-native metal catalysts for the sustainable synthesis of molecules for pharmaceutical, biotechnological and industrial purposes. Therefore, metalloenzymes are the relevant targets for the design of artificial biocatalysts. The search and development of new scaffolds capable of hosting metals with high levels of selectivity could significantly expand the scope of bio-catalysis. To meet this challenge, herein, three native scaffolds: [1Fe-4Cys] (rubredoxin), [3Fe-4S] (ferredoxin), and [S2MoS2CuS2MoS2]-ORP (orange protein) protein scaffolds are case studies describing templates for the synthesis of non-native monomeric to mixed metal–sulfur clusters, which mimic native Ni containing metalloenzymes including [Ni-Fe] Hydrogenase and [Ni-Fe] CO Dehydrogenase. The non-native metal-substituted metalloproteins are not only useful for catalysis but also as spectroscopic probes.

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Diverse biological roles of the tetrathiomolybdate anion

Maiti

Moura

2021

Coordination Chemistry Reviews

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Synthesis and characterization of [S2MoS2Cu(n-SPhF)]2−(n=o, m, p) clusters: Potential 19F-NMR structural probes for Orange Protein

Cited by 4 publications

References 28 publications

Molybdenum‐Copper Antagonism In Metalloenzymes And Anti‐Copper Therapy

Molybdenum‐Copper Antagonism In Metalloenzymes And Anti‐Copper Therapy

Native Protein Template Assisted Synthesis of Non-Native Metal-Sulfur Clusters

Diverse biological roles of the tetrathiomolybdate anion

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