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Items: 1 to 20 of 107


Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol cleavage reaction catalyzed by myo-inositol oxygenase.

Xing G, Barr EW, Diao Y, Hoffart LM, Prabhu KS, Arner RJ, Reddy CC, Krebs C, Bollinger JM Jr.

Biochemistry. 2006 May 2;45(17):5402-12.


Spectroscopic definition of the biferrous and biferric sites in de novo designed four-helix bundle DFsc peptides: implications for O2 reactivity of binuclear non-heme iron enzymes.

Bell CB, Calhoun JR, Bobyr E, Wei PP, Hedman B, Hodgson KO, Degrado WF, Solomon EI.

Biochemistry. 2009 Jan 13;48(1):59-73. doi: 10.1021/bi8016087.


A coupled dinuclear iron cluster that is perturbed by substrate binding in myo-inositol oxygenase.

Xing G, Hoffart LM, Diao Y, Prabhu KS, Arner RJ, Reddy CC, Krebs C, Bollinger JM Jr.

Biochemistry. 2006 May 2;45(17):5393-401.


Spectroscopic definition of the ferroxidase site in M ferritin: comparison of binuclear substrate vs cofactor active sites.

Schwartz JK, Liu XS, Tosha T, Theil EC, Solomon EI.

J Am Chem Soc. 2008 Jul 23;130(29):9441-50. doi: 10.1021/ja801251q. Epub 2008 Jun 25.


Spectroscopic studies of single and double variants of M ferritin: lack of conversion of a biferrous substrate site into a cofactor site for O2 activation.

Kwak Y, Schwartz JK, Haldar S, Behera RK, Tosha T, Theil EC, Solomon EI.

Biochemistry. 2014 Jan 28;53(3):473-82. doi: 10.1021/bi4013726. Epub 2014 Jan 15.


Structural, EPR, and Mössbauer characterization of (μ-alkoxo)(μ-carboxylato)diiron(II,III) model complexes for the active sites of mixed-valent diiron enzymes.

Li F, Chakrabarti M, Dong Y, Kauffmann K, Bominaar EL, Münck E, Que L Jr.

Inorg Chem. 2012 Mar 5;51(5):2917-29. doi: 10.1021/ic2021726. Epub 2012 Feb 23.


CD/MCD/VTVH-MCD Studies of Escherichia coli Bacterioferritin Support a Binuclear Iron Cofactor Site.

Kwak Y, Schwartz JK, Huang VW, Boice E, Kurtz DM Jr, Solomon EI.

Biochemistry. 2015 Dec 1;54(47):7010-8. doi: 10.1021/acs.biochem.5b01033. Epub 2015 Nov 18.


Demonstration by 2H ENDOR spectroscopy that myo-inositol binds via an alkoxide bridge to the mixed-valent diiron center of myo-inositol oxygenase.

Kim SH, Xing G, Bollinger JM Jr, Krebs C, Hoffman BM.

J Am Chem Soc. 2006 Aug 16;128(32):10374-5.


CD and MCD spectroscopic studies of the two Dps miniferritin proteins from Bacillus anthracis: role of O2 and H2O2 substrates in reactivity of the diiron catalytic centers.

Schwartz JK, Liu XS, Tosha T, Diebold A, Theil EC, Solomon EI.

Biochemistry. 2010 Dec 14;49(49):10516-25. doi: 10.1021/bi101346c. Epub 2010 Nov 12.


Spectroscopic and electronic structure studies of protocatechuate 3,4-dioxygenase: nature of tyrosinate-Fe(III) bonds and their contribution to reactivity.

Davis MI, Orville AM, Neese F, Zaleski JM, Lipscomb JD, Solomon EI.

J Am Chem Soc. 2002 Jan 30;124(4):602-14.


Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism.

Clay MD, Jenney FE Jr, Hagedoorn PL, George GN, Adams MW, Johnson MK.

J Am Chem Soc. 2002 Feb 6;124(5):788-805.


Activation of α-keto acid-dependent dioxygenases: application of an {FeNO}7/{FeO2}8 methodology for characterizing the initial steps of O2 activation.

Diebold AR, Brown-Marshall CD, Neidig ML, Brownlee JM, Moran GR, Solomon EI.

J Am Chem Soc. 2011 Nov 16;133(45):18148-60. doi: 10.1021/ja202549q. Epub 2011 Oct 21.


myo-Inositol oxygenase: a radical new pathway for O(2) and C-H activation at a nonheme diiron cluster.

Bollinger JM Jr, Diao Y, Matthews ML, Xing G, Krebs C.

Dalton Trans. 2009 Feb 14;(6):905-14. doi: 10.1039/b811885j. Epub 2008 Nov 26. Review.


Geometric and electronic structure of the Mn(IV)Fe(III) cofactor in class Ic ribonucleotide reductase: correlation to the class Ia binuclear non-heme iron enzyme.

Kwak Y, Jiang W, Dassama LM, Park K, Bell CB 3rd, Liu LV, Wong SD, Saito M, Kobayashi Y, Kitao S, Seto M, Yoda Y, Alp EE, Zhao J, Bollinger JM Jr, Krebs C, Solomon EI.

J Am Chem Soc. 2013 Nov 20;135(46):17573-84. doi: 10.1021/ja409510d. Epub 2013 Nov 6.


Spectroscopic studies of the mononuclear non-heme Fe(II) enzyme FIH: second-sphere contributions to reactivity.

Light KM, Hangasky JA, Knapp MJ, Solomon EI.

J Am Chem Soc. 2013 Jul 3;135(26):9665-74. doi: 10.1021/ja312571m. Epub 2013 Jun 20.

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