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1. Acid p K a Dependence in O–O Bond Heterolysis of a Nonheme Fe III –OOH Intermediate To Form a Potent Fe V ═O Oxidant with Heme Compound I-Like Reactivity

   https://doi.org/10.1021/jacs.9b08442  

   Xu, Shuangning ; Draksharapu, Apparao ; Rasheed, Waqas ; Que, Lawrence ( October 2019 , Journal of the American Chemical Society)
2. Sc 3+ -Promoted O–O Bond Cleavage of a (μ-1,2-Peroxo)diiron(III) Species Formed from an Iron(II) Precursor and O 2 to Generate a Complex with an Fe IV 2 (μ-O) 2 Core

   https://doi.org/10.1021/jacs.9b12081  

   Banerjee, Saikat ; Draksharapu, Apparao ; Crossland, Patrick M. ; Fan, Ruixi ; Guo, Yisong ; Swart, Marcel ; Que, Lawrence ( March 2020 , Journal of the American Chemical Society)
3. Reaction of O 2 with a diiron protein generates a mixed-valent Fe 2+ /Fe 3+ center and peroxide

   https://doi.org/10.1073/pnas.1809913116  

   Bradley, Justin M. ; Svistunenko, Dimitri A. ; Pullin, Jacob ; Hill, Natalie ; Stuart, Rhona K. ; Palenik, Brian ; Wilson, Michael T. ; Hemmings, Andrew M. ; Moore, Geoffrey R. ; Le Brun, Nick E. ( February 2019 , Proceedings of the National Academy of Sciences)

   The gene encoding the cyanobacterial ferritinSynFtn is up-regulated in response to copper stress. Here, we show that, whileSynFtn does not interact directly with copper, it is highly unusual in several ways. First, its catalytic diiron ferroxidase center is unlike those of all other characterized prokaryotic ferritins and instead resembles an animal H-chain ferritin center. Second, as demonstrated by kinetic, spectroscopic, and high-resolution X-ray crystallographic data, reaction of O₂with the di-Fe²⁺center results in a direct, one-electron oxidation to a mixed-valent Fe²⁺/Fe³⁺form. Iron–O₂chemistry of this type is currently unknown among the growing family of proteins that bind a diiron site within a four α-helical bundle in general and ferritins in particular. The mixed-valent form, which slowly oxidized to the more usual di-Fe³⁺form, is an intermediate that is continually generated during mineralization. Peroxide, rather than superoxide, is shown to be the product of O₂reduction, implying that ferroxidase centers function in pairs via long-range electron transfer through the protein resulting in reduction of O₂bound at only one of the centers. We show that electron transfer is mediated by the transient formation of a radical on Tyr40, which lies ∼4 Å from the diiron center. As well as demonstrating an expansion of the iron–O₂chemistry known to occur in nature, these data are also highly relevant to the question of whether all ferritins mineralize iron via a common mechanism, providing unequivocal proof that they do not.

    

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4. Enhanced magnetostrictive properties of nanocrystalline Dy 3+ substituted Fe-rich Co 0.8 Fe 2.2 O 4 for sensor applications

   https://doi.org/10.1063/1.5005519  

   Kharat, Shahaji P. ; Swadipta, Roy ; Kambale, R. C. ; Kolekar, Y. D. ; Ramana, C. V. ( October 2017 , Journal of Applied Physics)
5. NO and N 2 O Release from the Trityl Diazeniumdiolate Complexes [M(O 2 N 2 CPh 3 ) 3 ] − (M = Fe, Co)

   https://doi.org/10.1021/acs.inorgchem.2c04088  

   Baeza Cinco, Miguel Á. ; Chakraborty, Arunavo ; Guzman, Camilo F. ; Kräh, Sabrina ; Wu, Guang ; Hayton, Trevor W. ( March 2023 , Inorganic Chemistry)