916148-26-0

Basic information

• Product Name: [Fe(II)(1,4,8,12-tetraazacyclopentadecane)(SC₆H₅)]BF₄
• Synonyms: [Fe(II)(1,4,8,12-tetraazacyclopentadecane)(SC₆H₅)]BF₄
• CAS NO: 916148-26-0
• Molecular Weight: 466.178
• Mol File: 916148-26-0.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: [Fe(II)(1,4,8,12-tetraazacyclopentadecane)(SC₆H₅)]BF₄(CAS DataBase Reference)
• NIST Chemistry Reference: [Fe(II)(1,4,8,12-tetraazacyclopentadecane)(SC₆H₅)]BF₄(916148-26-0)
• EPA Substance Registry System: [Fe(II)(1,4,8,12-tetraazacyclopentadecane)(SC₆H₅)]BF₄(916148-26-0)

Safety Data

• Hazardous Substances Data: 916148-26-0(Hazardous Substances Data)

Upstream product

• 15439-16-4 1,4,8,12-Tetraazacyclopentadecan 
• 930-69-8 sodium thiophenolate 

Downstream Products

• 916148-30-6 [Fe(III)(1,4,8,12-tetraazacyclopentadecane)(SC₆H₅)(cumeneperoxo)]BF₄ 
• 916148-28-2 [Fe(III)(1,4,8,12-tetraazacyclopentadecane)(SC₆H₅)(t-butylperoxo)]BF₄ 
• 916148-30-6 [Fe(II)([15]aneN₄)(SC₆H₅)(OO-cumenyl)]BF₄ 
• 916148-28-2 [Fe(II)([15]aneN₄)(SC₆H₅)(OO-t-Bu)]BF₄ 
• 916148-33-9 [Fe(II)([15]aneN₄)(SC₆H₅)(⁽¹⁸⁾O⁽¹⁸⁾O-t-Bu)]BF₄ 

Relevant articles and documents

Rational tuning of the thiolate donor in model complexes of superoxide reductase: Direct evidence for a trans influence in FeIII-OOR complexes

Iron peroxide species have been identified as important intermediates in a number of nonheme iron as well as heme-containing enzymes, yet there are only a few examples of such species either synthetic or biological that have been well characterized. We describe the synthesis and structural characterization of a new series of five-coordinate (N4S(thiolate))FeII complexes that react with tert-butyl hydroperoxide (tBuOOH) or cumenyl hydroperoxide (CmOOH) to give metastable alkylperoxo-iron(III) species (N4S(thiolate)FeIII-OOR) at low temperature. These complexes were designed specifically to mimic the nonheme iron active site of superoxide reductase, which contains a five-coordinate iron(II) center bound by one Cys and four His residues in the active form of the protein. The structures of the FeII complexes are analyzed by X-ray crystallography, and their electrochemical properties are assessed by cyclic voltammetry. For the FeIII-OOR species, low-temperature UV-vis spectra reveal intense peaks between 500-550 nm that are typical of peroxide to iron(III) ligand-to-metal charge-transfer (LMCT) transitions, and EPR spectroscopy shows that these alkylperoxo species are all low-spin iron(III) complexes. Identification of the vibrational modes of the FeIII-OOR unit comes from resonance Raman (RR) spectroscopy, which shows ν(Fe-O) modes between 600-635 cm-1 and ν(O-O) bands near 800 cm-1. These Fe-O stretching frequencies are significantly lower than those found in other low-spin FeIII-OOR complexes. Trends in the data conclusively show that this weakening of the Fe-O bond arises from a trans influence of the thiolate donor, and density functional theory (DFT) calculations support these findings. These results suggest a role for the cysteine ligand in SOR, and are discussed in light of the recent assessments of the function of the cysteine ligand in this enzyme.