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Coordination Chemistry in the Biosphere and Geosphere
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Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase
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Borgstahl G.E.O., Pokross M., Chehab R., Sekher A., Snell E.H. Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase. J Mol Biol. 296:2000;951-959.
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Fe-superoxide dismutase
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Edited by Wieghardt K, Huber R, Poulos TL, Messerschmidt A: Chicester, New York, Weinheim, Brisbane, Singapore and Toronto: Wiley and Sons;
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Miller A-F: Fe-superoxide dismutase. In Handbook of Metalloproteins, vol. 1. Edited by Wieghardt K, Huber R, Poulos TL, Messerschmidt A: Chicester, New York, Weinheim, Brisbane, Singapore and Toronto: Wiley and Sons; 2001:668-682.
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Miller, A.-F.1
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0038682379
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7 system: Exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase
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A long-overdue investigation of Fe-SOD's reactivity with NO, which is a uniquely faithful substrate analogue with respect to its electronic structure and redox activity.
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7 system: exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase. J Am Chem Soc. 125:2003;8348-8363 A long-overdue investigation of Fe-SOD's reactivity with NO, which is a uniquely faithful substrate analogue with respect to its electronic structure and redox activity.
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J Am Chem Soc
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Jackson, T.A.1
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Steady-state kinetic studies of superoxide dismutases: Properties of the iron containing protein from Escherichia coli
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Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase
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Miller A-F., Padmakumar K., Sorkin D.L., Karapetian A., Vance C.K. Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase. J Inorg Biochem. 93:2003;71-83.
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Coupled redox potentials in manganese and iron superoxide dismutases from reaction kinetics and density functional/electrostatics calculations
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Detailed computations comparing the energetics of metal ion reduction alone and coupled to proton transfer, from an expert. This paper duplicates trends observed among different Fe- and Mn-SODs and validates the expected link between observed rate constants and the reduction midpoint potential.
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Han W.G., Lovell T., Noodleman L. Coupled redox potentials in manganese and iron superoxide dismutases from reaction kinetics and density functional/electrostatics calculations. Inorg Chem. 41:2002;205-218 Detailed computations comparing the energetics of metal ion reduction alone and coupled to proton transfer, from an expert. This paper duplicates trends observed among different Fe- and Mn-SODs and validates the expected link between observed rate constants and the reduction midpoint potential.
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Han, W.G.1
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Second-sphere contributions to substrate analog binding in iron(III) superoxide dismutase
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Xie J., Yikilmaz E., Miller A-F., Brunold T.C. Second-sphere contributions to substrate analog binding in iron(III) superoxide dismutase. J Am Chem Soc. 124:2002;3769-3774.
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The 1.6 Å resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus
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Kerfeld C.A., Yoshida S., Tran K.T., Yeates T.O., Cascio D., Bottin H., Berthomieu C., Sugiura M., Boussac A. The 1.6 Å resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus. J Biol Inorg Chem. 8:2003;707-714.
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0037063508
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Spectroscopic and computational studies on iron and manganese superoxide dismutases: Nature of the chemical events associated with active site pKs
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Jackson T.A., Xie J., Yikilmaz E., Miller A-F., Brunold T.C. Spectroscopic and computational studies on iron and manganese superoxide dismutases: nature of the chemical events associated with active site pKs. J Am Chem Soc. 124:2002;10833-10845.
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0037132612
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Comparison and contrasts between the active site pKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase
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Despite the overwhelming appearance of similarity between the active sites of Fe-SOD and MnSOD, the events responsible for the oxidized state pK are not the same. The mechanistic significance of this finding is discussed.
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Maliekal J., Karapetian A., Vance C., Yikilmaz E., Wu Q., Jackson T., Brunold T.C., Spiro T.G., Miller A-F. Comparison and contrasts between the active site pKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase. J Am Chem Soc. 124:2002;15064-15075 Despite the overwhelming appearance of similarity between the active sites of Fe-SOD and MnSOD, the events responsible for the oxidized state pK are not the same. The mechanistic significance of this finding is discussed.
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Sorkin D.L., Duong D.K., Miller A-F. Mutation of tyrosine 34 to phenylalanine eliminates the active site pK of reduced Fe-SOD. Biochemistry. 36:1997;8202-8208.
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Tabares L.C., Bittel C., Carrillo N., Bortolotti A., Cortez N. The single superoxide dismutase of Rhodobacter capsulatus is a cambialistic, manganese-containing enzyme. J Bacteriol. 185:2003;3223-3227.
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A thoughtful comparison of several mutants addressing the Gln that hydrogen bonds to coordinated solvent, as well as the 'gateway' Tyr.
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Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., Jameson G.B. Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase. Biochemistry. 40:2001;15-27 A thoughtful comparison of several mutants addressing the Gln that hydrogen bonds to coordinated solvent, as well as the 'gateway' Tyr.
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Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site
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A lesson in the subtlety of proteins, and enzyme active sites. A remote mutation indirectly modifies the strengths of hydrogen bonds and thus achieves a 20-fold effect on activity. This most recent contribution from one of the founders of the field combines biochemical, spectroscopic and structural data.
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Yamakura F., Sugio S., Hiraoka B.Y., Ohmori D., Yokota T. Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site. Biochemistry. 42:2003;10790-10799 A lesson in the subtlety of proteins, and enzyme active sites. A remote mutation indirectly modifies the strengths of hydrogen bonds and thus achieves a 20-fold effect on activity. This most recent contribution from one of the founders of the field combines biochemical, spectroscopic and structural data.
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0032554625
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Spectroscopic comparisons of the pH dependencies of Fe-substituted-(Mn) superoxide dismutase and Fe-superoxide dismutase
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Vance C.K., Miller A-F. Spectroscopic comparisons of the pH dependencies of Fe-substituted-(Mn) superoxide dismutase and Fe-superoxide dismutase. Biochemistry. 37:1998;5518-5527.
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0037046112
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Biochemical and electron paramagnetic resonance study of the iron superoxide dismutase from Plasmodium falciparum
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A simple proposal that can explain the inactivity of metal-substituted superoxide dismutases
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Mutational and spectroscopic studies of the significance of the active site Gln to metal ion specificity in superoxide dismutase
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Schwartz A.L., Yikilmaz E., Vance C.K., Vathyam S., Koder R.L. Jr., Miller A.-F. Mutational and spectroscopic studies of the significance of the active site Gln to metal ion specificity in superoxide dismutase. J Inorg Biochem. 80:2000;247-256.
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0037051599
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Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase
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Demonstration of a strongly elevated reduction potential despite preservation of native-like iron electronics in both oxidation states, as a result of conversion of an active site hydrogen bond donor into a hydrogen bond acceptor
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Yikilmaz E., Xie J., Miller A-F., Brunold T.C. Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase. J Am Chem Soc. 124:2002;3482-3483 Demonstration of a strongly elevated reduction potential despite preservation of native-like iron electronics in both oxidation states, as a result of conversion of an active site hydrogen bond donor into a hydrogen bond acceptor.
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Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: Insertion of valine Cγ into the substrate access channel
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