334678-07-8

Basic information

• Product Name: (C₂H₅)4N⁽¹⁺⁾*Mo(C₆F₅O)(S₂C₂(CH₃)2)2^(1-)=(C₂H₅)4NMo(C₆F₅O)(CH₃C₂S₂CH₃)2
• Synonyms: (C₂H₅)4N⁽¹⁺⁾*Mo(C₆F₅O)(S₂C₂(CH₃)2)2^(1-)=(C₂H₅)4NMo(C₆F₅O)(CH₃C₂S₂CH₃)2
• CAS NO: 334678-07-8
• Molecular Weight: 645.698
• Mol File: 334678-07-8.mol

Chemical Properties

• CAS DataBase Reference: (C₂H₅)4N⁽¹⁺⁾*Mo(C₆F₅O)(S₂C₂(CH₃)2)2^(1-)=(C₂H₅)4NMo(C₆F₅O)(CH₃C₂S₂CH₃)2(CAS DataBase Reference)
• NIST Chemistry Reference: (C₂H₅)4N⁽¹⁺⁾*Mo(C₆F₅O)(S₂C₂(CH₃)2)2^(1-)=(C₂H₅)4NMo(C₆F₅O)(CH₃C₂S₂CH₃)2(334678-07-8)
• EPA Substance Registry System: (C₂H₅)4N⁽¹⁺⁾*Mo(C₆F₅O)(S₂C₂(CH₃)2)2^(1-)=(C₂H₅)4NMo(C₆F₅O)(CH₃C₂S₂CH₃)2(334678-07-8)

Safety Data

• Hazardous Substances Data: 334678-07-8(Hazardous Substances Data)

Upstream product

• 227468-58-8 (C₂H₅)4N⁽¹⁺⁾*C₆F₅O^(1-)=(C₂H₅)4NOC₆F₅ 

Relevant articles and documents

Bis(dithiolene)molybdenum analogues relevant to the DMSO reductase enzyme family: Synthesis, structures, and oxygen atom transfer reactions and kinetics

A series of dithiolene complexes of the general type [MoIV(QR′)(S2C2Me2) 2]1- has been prepared and structurally characterized as possible structural and reactivity analogues of reduced sites of the enzymes DMSOR and TMAOR (QR' = PhO-, 2-AdO-, PriO-), dissimilatory nitrate reductase (QR' = 2-ADS-), and formate dehydrogenase (QR' = 2-AdSe-). The complexes are square pyramidal with the molybdenum atom positioned 0.74-0.80 A above the S4 mean plane toward axial ligand QR'. In part on the basis of a recent clarification of the active site of oxidized Rhodobacter sphaeroides DMSOR (Li, H.-K.; Temple, C.; Rajagopalan, K, V.; Schindelin, H. J. Am. Chem. Soc. 2000, 122, 7673), we have adopted the minimal reaction paradigm MoIV + XO ? MoIVO + X involving desoxo Mo(IV), monooxo Mo(VI), and substrate/product XO/X for direct oxygen atom transfer of DMSOR and TMAOR enzymes. The [Mo(OR')(S2C2Me2)2]I- species carry dithiolene and anionic oxygen ligands intended to simulate cofactor ligand and serinate binding in DMSOR and TMAOR catalytic sites. In systems with N-oxide and S-oxide substrates, the observed overall reaction sequence is [MoIV(OR')(S2C2Me2) 2]I- + XO → [MoIVO(OR')(S2C2Me2) 2]I- →[MoVO(S2C2Me2) 2]I-. Direct oxo transfer in the first step has been proven by isotope labeling. The reactivity of [Mo(OPh)(S2C2Me2)2]I- (1) has been the most extensively studied. In second-order reactions, 1 reduces DMSO and (CH2)4SO (k2 ≈ 10-6, 10-4 M-I s-I; ΔS? = -36, -39 eu) and Me3NO (k2 = 200 M-I s-I; ΔS? = -21 eu) in acetonitrile at 298 K. Activation entropies indicate an associative transition state, which from relative rates and substrate properties is inferred to be concerted with X-O bond weakening and Mo-O bond making. The MoVIO product in the first step, such as [MoVIO(OR')(S2C2Me2) 2]I-, is an intermediate in the overall reaction sequence, in as much as it is too unstable to isolate and decays by an internal redox process to a MoVO product, liberating an equimolar quantity of phenol. This research affords the first analogue reaction systems of biological N-oxide and S-oxide substrates that are based on desoxo Mo(IV) complexes with biologically relevant coordination. Oxo-transfer reactions in analogue systems are substantially slower than enzyme systems based on a kcat/KM criterion. An interpretation of this behavior requires more information on the rate-limiting step(s) in enzyme catalytic cycles. (2-Ad = 2-adamantyl, DMSOR = dimethyl sulfoxide reductase, TMAOR = trimethylamine N-oxide reductase).