| Year |
Citation |
Score |
| 2010 |
Miller AF, Yikilmaz E, Vathyam S. 15N-NMR characterization of His residues in and around the active site of FeSOD. Biochimica Et Biophysica Acta. 1804: 275-84. PMID 19931430 DOI: 10.1016/J.Bbapap.2009.11.009 |
0.701 |
|
| 2008 |
Grove LE, Xie J, Yikilmaz E, Miller AF, Brunold TC. Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase. Inorganic Chemistry. 47: 3978-92. PMID 18433120 DOI: 10.1021/Ic702412Y |
0.752 |
|
| 2008 |
Grove LE, Xie J, Yikilmaz E, Karapetyan A, Miller AF, Brunold TC. Spectroscopic and computational insights into second-sphere amino-acid tuning of substrate analogue/active-site interactions in iron(III) superoxide dismutase. Inorganic Chemistry. 47: 3993-4004. PMID 18433119 DOI: 10.1021/Ic702414M |
0.725 |
|
| 2008 |
Schwartz AL, Yikilmaz E, Vance CK, Vathyam S, Koder RL, Miller AF. Corrigendum to: "Mutational and spectroscopic studies of the significance of the active site glutamine to metal ion specificity in superoxide dismutase [Journal of Inorganic Biochemistry 80 (2000) 247]" (DOI:10.1016/S0162-0134(00)00086-6) Journal of Inorganic Biochemistry. 102: 992. DOI: 10.1016/J.Jinorgbio.2007.11.001 |
0.667 |
|
| 2007 |
Yikilmaz E, Porta J, Grove LE, Vahedi-Faridi A, Bronshteyn Y, Brunold TC, Borgstahl GE, Miller AF. How can a single second sphere amino acid substitution cause reduction midpoint potential changes of hundreds of millivolts? Journal of the American Chemical Society. 129: 9927-40. PMID 17628062 DOI: 10.1021/Ja069224T |
0.739 |
|
| 2006 |
Yikilmaz E, Rodgers DW, Miller AF. The crucial importance of chemistry in the structure-function link: Manipulating hydrogen bonding in iron-containing superoxide dismutase Biochemistry. 45: 1151-1161. PMID 16430211 DOI: 10.1021/Bi051495D |
0.719 |
|
| 2003 |
Jackson TA, Yikilmaz E, Miller AF, Brunold TC. Spectroscopic and computational study of a non-heme iron [Fe-NO]7 system: exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase. Journal of the American Chemical Society. 125: 8348-63. PMID 12837107 DOI: 10.1021/Ja029523S |
0.708 |
|
| 2002 |
Maliekal J, Karapetian A, Vance C, Yikilmaz E, Wu Q, Jackson T, Brunold TC, Spiro TG, Miller AF. Comparison and contrasts between the active site PKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase. Journal of the American Chemical Society. 124: 15064-75. PMID 12475351 DOI: 10.1021/Ja027319Z |
0.734 |
|
| 2002 |
Jackson TA, Xie J, Yikilmaz E, Miller AF, Brunold TC. Spectroscopic and computational studies on iron and manganese superoxide dismutases: nature of the chemical events associated with active-site pKs. Journal of the American Chemical Society. 124: 10833-45. PMID 12207539 DOI: 10.1021/Ja0266058 |
0.664 |
|
| 2002 |
Xie J, Yikilmaz E, Miller AF, Brunold TC. Second-sphere contributions to substrate-analogue binding in iron(III) superoxide dismutase. Journal of the American Chemical Society. 124: 3769-74. PMID 11929267 DOI: 10.1021/Ja016254H |
0.645 |
|
| 2002 |
Yikilmaz E, Xie J, Brunold TC, Miller AF. Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase. Journal of the American Chemical Society. 124: 3482-3. PMID 11929218 DOI: 10.1021/Ja011220V |
0.73 |
|
| 2000 |
Schwartz AL, Yikilmaz E, Vance CK, Vathyam S, Koder RL, Miller AF. Mutational and spectroscopic studies of the significance of the active site glutamine to metal ion specificity in superoxide dismutase. Journal of Inorganic Biochemistry. 80: 247-56. PMID 11001096 DOI: 10.1016/S0162-0134(00)00086-6 |
0.721 |
|
| 1999 |
Campbell KA, Yikilmaz E, Grant CV, Gregor W, Miller AF, Britt RD. Parallel polarization EPR characterization of the Mn(III) center of oxidized manganese superoxide dismutase Journal of the American Chemical Society. 121: 4714-4715. DOI: 10.1021/Ja9902219 |
0.576 |
|
| Show low-probability matches. |