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  • 1
    Publication Date: 2011-10-28
    Description: Oxygen-containing mononuclear iron species--iron(III)-peroxo, iron(III)-hydroperoxo and iron(IV)-oxo--are key intermediates in the catalytic activation of dioxygen by iron-containing metalloenzymes. It has been difficult to generate synthetic analogues of these three active iron-oxygen species in identical host complexes, which is necessary to elucidate changes to the structure of the iron centre during catalysis and the factors that control their chemical reactivities with substrates. Here we report the high-resolution crystal structure of a mononuclear non-haem side-on iron(III)-peroxo complex, [Fe(III)(TMC)(OO)](+). We also report a series of chemical reactions in which this iron(III)-peroxo complex is cleanly converted to the iron(III)-hydroperoxo complex, [Fe(III)(TMC)(OOH)](2+), via a short-lived intermediate on protonation. This iron(III)-hydroperoxo complex then cleanly converts to the ferryl complex, [Fe(IV)(TMC)(O)](2+), via homolytic O-O bond cleavage of the iron(III)-hydroperoxo species. All three of these iron species--the three most biologically relevant iron-oxygen intermediates--have been spectroscopically characterized; we note that they have been obtained using a simple macrocyclic ligand. We have performed relative reactivity studies on these three iron species which reveal that the iron(III)-hydroperoxo complex is the most reactive of the three in the deformylation of aldehydes and that it has a similar reactivity to the iron(IV)-oxo complex in C-H bond activation of alkylaromatics. These reactivity results demonstrate that iron(III)-hydroperoxo species are viable oxidants in both nucleophilic and electrophilic reactions by iron-containing enzymes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3306242/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3306242/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Jaeheung -- Jeon, Sujin -- Wilson, Samuel A -- Liu, Lei V -- Kang, Eun A -- Braymer, Joseph J -- Lim, Mi Hee -- Hedman, Britt -- Hodgson, Keith O -- Valentine, Joan Selverstone -- Solomon, Edward I -- Nam, Wonwoo -- 5P41RR001209/RR/NCRR NIH HHS/ -- GM 40392/GM/NIGMS NIH HHS/ -- P41 RR001209/RR/NCRR NIH HHS/ -- P41 RR001209-31/RR/NCRR NIH HHS/ -- R01 GM040392/GM/NIGMS NIH HHS/ -- R01 GM040392-25/GM/NIGMS NIH HHS/ -- RR-001209/RR/NCRR NIH HHS/ -- England -- Nature. 2011 Oct 26;478(7370):502-5. doi: 10.1038/nature10535.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bioinspired Science, Ewha Womans University, Seoul 120-750, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22031443" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehydes/metabolism ; Crystallography, X-Ray ; Enzymes/chemistry/metabolism ; Hydrogen Peroxide/*chemistry/metabolism ; Iron/*chemistry/metabolism ; Ligands ; Models, Molecular ; Nonheme Iron Proteins/chemistry/metabolism ; Oxygen/chemistry/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1996-01-26
    Description: A subset of individuals with familial amyotrophic lateral sclerosis (FALS) possesses dominantly inherited mutations in the gene that encodes copper-zinc superoxide dismutase (CuZnSOD). A4V and G93A, two of the mutant enzymes associated with FALS, were shown to catalyze the oxidation of a model substrate (spin trap 5,5'-dimethyl-1-pyrroline N-oxide) by hydrogen peroxide at a higher rate than that seen with the wild-type enzyme. Catalysis of this reaction by A4V and G93A was more sensitive to inhibition by the copper chelators diethyldithiocarbamate and penicillamine than was catalysis by wild-type CuZnSOD. The same two chelators reversed the apoptosis-inducing effect of mutant enzymes expressed in a neural cell line. These results suggest that oxidative reactions catalyzed by mutant CuZnSOD enzymes initiate the neuropathologic changes in FALS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wiedau-Pazos, M -- Goto, J J -- Rabizadeh, S -- Gralla, E B -- Roe, J A -- Lee, M K -- Valentine, J S -- Bredesen, D E -- AG12282/AG/NIA NIH HHS/ -- DK46828/DK/NIDDK NIH HHS/ -- GM28222/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):515-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560268" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*enzymology/genetics ; Animals ; Apoptosis/drug effects ; Binding Sites ; Catalysis ; Cell Line ; Chelating Agents/pharmacology ; Copper/metabolism ; Cyclic N-Oxides/metabolism ; Ditiocarb/pharmacology ; Humans ; Hydrogen Peroxide/metabolism ; Mutation ; Oxidation-Reduction ; Penicillamine/pharmacology ; Rats ; Superoxide Dismutase/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2004-08-25
    Description: We demonstrate that the cell wall of living Saccharomyces cerevisiae (baker's yeast) exhibits local temperature-dependent nanomechanical motion at characteristic frequencies. The periodic motions in the range of 0.8 to 1.6 kHz with amplitudes of approximately 3 nm were measured using the cantilever of an atomic force microscope (AFM). Exposure of the cells to a metabolic inhibitor causes the periodic motion to cease. From the strong frequency dependence on temperature, we derive an activation energy of 58 kJ/mol, which is consistent with the cell's metabolism involving molecular motors such as kinesin, dynein, and myosin. The magnitude of the forces observed ( approximately 10 nN) suggests concerted nanomechanical activity is operative in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelling, Andrew E -- Sehati, Sadaf -- Gralla, Edith B -- Valentine, Joan S -- Gimzewski, James K -- DK46828/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1147-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15326353" target="_blank"〉PubMed〈/a〉
    Keywords: Biomechanical Phenomena ; Cell Wall/*physiology/ultrastructure ; Fourier Analysis ; Microscopy, Atomic Force ; Motion ; Movement ; Saccharomyces cerevisiae/drug effects/*physiology/ultrastructure ; Sodium Azide/pharmacology ; Temperature
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2010-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gleick, P H -- Adams, R M -- Amasino, R M -- Anders, E -- Anderson, D J -- Anderson, W W -- Anselin, L E -- Arroyo, M K -- Asfaw, B -- Ayala, F J -- Bax, A -- Bebbington, A J -- Bell, G -- Bennett, M V L -- Bennetzen, J L -- Berenbaum, M R -- Berlin, O B -- Bjorkman, P J -- Blackburn, E -- Blamont, J E -- Botchan, M R -- Boyer, J S -- Boyle, E A -- Branton, D -- Briggs, S P -- Briggs, W R -- Brill, W J -- Britten, R J -- Broecker, W S -- Brown, J H -- Brown, P O -- Brunger, A T -- Cairns, J Jr -- Canfield, D E -- Carpenter, S R -- Carrington, J C -- Cashmore, A R -- Castilla, J C -- Cazenave, A -- Chapin, F S 3rd -- Ciechanover, A J -- Clapham, D E -- Clark, W C -- Clayton, R N -- Coe, M D -- Conwell, E M -- Cowling, E B -- Cowling, R M -- Cox, C S -- Croteau, R B -- Crothers, D M -- Crutzen, P J -- Daily, G C -- Dalrymple, G B -- Dangl, J L -- Darst, S A -- Davies, D R -- Davis, M B -- De Camilli, P V -- Dean, C -- DeFries, R S -- Deisenhofer, J -- Delmer, D P -- DeLong, E F -- DeRosier, D J -- Diener, T O -- Dirzo, R -- Dixon, J E -- Donoghue, M J -- Doolittle, R F -- Dunne, T -- Ehrlich, P R -- Eisenstadt, S N -- Eisner, T -- Emanuel, K A -- Englander, S W -- Ernst, W G -- Falkowski, P G -- Feher, G -- Ferejohn, J A -- Fersht, A -- Fischer, E H -- Fischer, R -- Flannery, K V -- Frank, J -- Frey, P A -- Fridovich, I -- Frieden, C -- Futuyma, D J -- Gardner, W R -- Garrett, C J R -- Gilbert, W -- Goldberg, R B -- Goodenough, W H -- Goodman, C S -- Goodman, M -- Greengard, P -- Hake, S -- Hammel, G -- Hanson, S -- Harrison, S C -- Hart, S R -- Hartl, D L -- Haselkorn, R -- Hawkes, K -- Hayes, J M -- Hille, B -- Hokfelt, T -- House, J S -- Hout, M -- Hunten, D M -- Izquierdo, I A -- Jagendorf, A T -- Janzen, D H -- Jeanloz, R -- Jencks, C S -- Jury, W A -- Kaback, H R -- Kailath, T -- Kay, P -- Kay, S A -- Kennedy, D -- Kerr, A -- Kessler, R C -- Khush, G S -- Kieffer, S W -- Kirch, P V -- Kirk, K -- Kivelson, M G -- Klinman, J P -- Klug, A -- Knopoff, L -- Kornberg, H -- Kutzbach, J E -- Lagarias, J C -- Lambeck, K -- Landy, A -- Langmuir, C H -- Larkins, B A -- Le Pichon, X T -- Lenski, R E -- Leopold, E B -- Levin, S A -- Levitt, M -- Likens, G E -- Lippincott-Schwartz, J -- Lorand, L -- Lovejoy, C O -- Lynch, M -- Mabogunje, A L -- Malone, T F -- Manabe, S -- Marcus, J -- Massey, D S -- McWilliams, J C -- Medina, E -- Melosh, H J -- Meltzer, D J -- Michener, C D -- Miles, E L -- Mooney, H A -- Moore, P B -- Morel, F M M -- Mosley-Thompson, E S -- Moss, B -- Munk, W H -- Myers, N -- Nair, G B -- Nathans, J -- Nester, E W -- Nicoll, R A -- Novick, R P -- O'Connell, J F -- Olsen, P E -- Opdyke, N D -- Oster, G F -- Ostrom, E -- Pace, N R -- Paine, R T -- Palmiter, R D -- Pedlosky, J -- Petsko, G A -- Pettengill, G H -- Philander, S G -- Piperno, D R -- Pollard, T D -- Price, P B Jr -- Reichard, P A -- Reskin, B F -- Ricklefs, R E -- Rivest, R L -- Roberts, J D -- Romney, A K -- Rossmann, M G -- Russell, D W -- Rutter, W J -- Sabloff, J A -- Sagdeev, R Z -- Sahlins, M D -- Salmond, A -- Sanes, J R -- Schekman, R -- Schellnhuber, J -- Schindler, D W -- Schmitt, J -- Schneider, S H -- Schramm, V L -- Sederoff, R R -- Shatz, C J -- Sherman, F -- Sidman, R L -- Sieh, K -- Simons, E L -- Singer, B H -- Singer, M F -- Skyrms, B -- Sleep, N H -- Smith, B D -- Snyder, S H -- Sokal, R R -- Spencer, C S -- Steitz, T A -- Strier, K B -- Sudhof, T C -- Taylor, S S -- Terborgh, J -- Thomas, D H -- Thompson, L G -- Tjian, R T -- Turner, M G -- Uyeda, S -- Valentine, J W -- Valentine, J S -- Van Etten, J L -- van Holde, K E -- Vaughan, M -- Verba, S -- von Hippel, P H -- Wake, D B -- Walker, A -- Walker, J E -- Watson, E B -- Watson, P J -- Weigel, D -- Wessler, S R -- West-Eberhard, M J -- White, T D -- Wilson, W J -- Wolfenden, R V -- Wood, J A -- Woodwell, G M -- Wright, H E Jr -- Wu, C -- Wunsch, C -- Zoback, M L -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 May 7;328(5979):689-90. doi: 10.1126/science.328.5979.689.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20448167" target="_blank"〉PubMed〈/a〉
    Keywords: *Climate Change ; Politics ; Public Policy ; Research/standards ; Research Personnel
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valentine, J S -- New York, N.Y. -- Science. 1992 Jun 19;256(5064):1615.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17841076" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1992-02-28
    Description: Novel sol-gel synthetic techniques were used to immobilize copper-zinc superoxide dismutase (CuZnSOD), cytochrome c, and myoglobin (Mb) by encapsulation in stable, optically transparent, porous silica glass matrices under mild conditions such that the biomolecules retained their characteristic reactivities and spectroscopic properties. The resulting glasses allowed transport of small molecules into and out of the glasses at reasonable rates but nevertheless retained the protein molecules within their pores. Chemical reactions of the immobilized proteins could be monitored by means of changes in their visible absorption spectra. Silica glasses containing the immobilized proteins were observed to have similar reactivities and spectroscopic properties to those found for the proteins in solution. For example, encapsulated CuZnSOD was demetallated and remetallated, encapsulated ferricytochrome c was reduced and then reoxidized, and encapsulated met Mb was reduced to deoxy Mb and then reacted either with dioxygen to make oxy Mb or with carbon monoxide to make carbonyl Mb.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellerby, L M -- Nishida, C R -- Nishida, F -- Yamanaka, S A -- Dunn, B -- Valentine, J S -- Zink, J I -- GM28222/GM/NIGMS NIH HHS/ -- T32 GM08375/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1113-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312257" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cytochrome c Group/chemistry ; Gels ; *Glass ; Horses ; Myoglobin/chemistry ; Proteins/*chemistry ; Solutions ; Spectrum Analysis ; Superoxide Dismutase/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1993-11-19
    Description: The proto-oncogene bcl-2 inhibits apoptotic and necrotic neural cell death. Expression of Bcl-2 in the GT1-7 neural cell line prevented death as a result of glutathione depletion. Intracellular reactive oxygen species and lipid peroxides rose rapidly in control cells depleted of glutathione, whereas cells expressing Bcl-2 displayed a blunted increase and complete survival. Modulation of the increase in reactive oxygen species influenced the degree of cell death. Yeast mutants null for superoxide dismutase were partially rescued by expression of Bcl-2. Thus, Bcl-2 prevents cell death by decreasing the net cellular generation of reactive oxygen species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kane, D J -- Sarafian, T A -- Anton, R -- Hahn, H -- Gralla, E B -- Valentine, J S -- Ord, T -- Bredesen, D E -- GM 28222/GM/NIGMS NIH HHS/ -- NS27812/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1274-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235659" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antioxidants/pharmacology ; Buthionine Sulfoximine ; *Cell Death ; Cell Line ; Glutathione/metabolism ; Hydroxyl Radical/metabolism ; Iron/metabolism ; Lipid Peroxidation ; Methionine Sulfoximine/analogs & derivatives/pharmacology ; Neurons/*cytology/metabolism ; Proto-Oncogene Proteins/*physiology ; Proto-Oncogene Proteins c-bcl-2 ; Reactive Oxygen Species/*metabolism ; Saccharomyces cerevisiae/growth & development/metabolism ; Superoxide Dismutase/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valentine, J S -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1617.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17808173" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valentine, J S -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1614.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17808150" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valentine, J S -- Gralla, E B -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):817-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095-1569, USA. jsv@chem.ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381192" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; *Carrier Proteins ; *Cation Transport Proteins ; Copper/*metabolism ; Fungal Proteins/*metabolism ; Humans ; Membrane Proteins/metabolism ; *Molecular Chaperones ; Saccharomyces cerevisiae/*metabolism ; *Saccharomyces cerevisiae Proteins ; Superoxide Dismutase/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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