Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii [PDF]
Journal of the American Chemical Society, American Chemical
Society, 2002, pp.4966-7, 2015 The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. It specifically reduces superoxide to produce H2O2. Here, we have reacted the SOR from Desulfoarculus baarsii directly with H2O2.
arxiv
Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis [PDF]
Biochemistry, American Chemical Society, 2001, pp.5032-40, 2015 Superoxide reductase (SOR) is a small metalloenzyme that catalyzes reduction of O(2)(*)(-) to H(2)O(2) and thus provides an antioxidant mechanism against superoxide radicals. Its active site contains an unusual mononuclear ferrous center, which is very efficient during electron transfer to O(2)(*)(-) [Lombard, M., Fontecave, M., Touati, D., and Nivi ...
arxiv
Studies on the succinate–neotetrazolium reductase system. Activation by vitamin K3 [PDF]
, 1959 T. F. Slater
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Fe(3+)-eta(2)-peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii [PDF]
Biophysical Chemistry, Elsevier, 2006, pp.38-48, 2015 Superoxide reductases (SORs) are superoxide (O2-)-detoxifying enzymes that catalyse the reduction of O2- into hydrogen peroxide. Three different classes of SOR have been reported on the basis of the presence or not of an additional N-terminal domain. They all share a similar active site, with an unusual non-heme Fe atom coordinated by four equatorial ...
arxiv
Enzymic studies of X-irradiated cornea and lens with special reference to glutathione reductase [PDF]
, 1959 Robert E. Kuhlman, Robert A. Resnik
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Fe3+-hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes [PDF]
Journal of the American Chemical Society, American Chemical
Society, 2005, pp.16436-41, 2014 Superoxide reductase (SOR) catalyzes the reduction of O2*- to H2O2. Its active site consists of a non-heme Fe2+ center in an unusual square-pyramidal [His4 Cys] coordination. Like many SORs, the electronic absorption band corresponding to the oxidized active site of the SOR from Desulfoarculus baarsii exhibits a pH-dependent alkaline transition ...
arxiv
Studies on the Nitrate Reductase of Escherichia Coli in the Cell-Free State [PDF]
, 1950 Wolfgang K. Joklik
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Evolutionary dynamics determines adaptation to inactivation of an essential gene [PDF]
arXiv, 2019 Genetic inactivation of essential genes creates an evolutionary scenario distinct from escape from drug inhibition, but the mechanisms of microbe adaptations in such cases remain unknown. Here we inactivate E. coli dihydrofolate reductase (DHFR) by introducing D27G,N,F chromosomal mutations in a key catalytic residue with subsequent adaptation by ...
arxiv
Note on the reactivation of reductase in washed yeast preparations [PDF]
, 1931 Arthur Harden, Marjorie G. Macfarlane
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THE INDUCED FORMATION OF NITRATE REDUCTASE IN AUXOTROPHIC MUTANTS OF ESCHERICHIA COLI [PDF]
, 1956 S. D. Wainwright, Ann Nevill
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