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Anne-Frances Miller - Publications

Affiliations: 
Johns Hopkins University, Baltimore, MD 
Area:
Microbiology Biology, Biochemistry, Molecular Biology
Website:
https://chem.as.uky.edu/users/afm
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61 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Duan HD, Mohamed-Raseek N, Miller AF. Spectroscopic evidence for direct flavin-flavin contact in a bifurcating electron transfer flavoprotein. The Journal of Biological Chemistry. PMID 32661195 DOI: 10.1074/Jbc.Ra120.013174  0.319
2020 Pitsawong W, Chenprakhon P, Dhammaraj T, Medhanavyn D, Sucharitakul J, Tonsook C, van Berkel WJH, Chaiyen P, Miller AF. Tuning of pKs activates substrates in flavin-dependent aromatic hydroxylases. The Journal of Biological Chemistry. PMID 32014994 DOI: 10.1074/Jbc.Ra119.011884  0.329
2019 Mohamed-Raseek N, Duan HD, Hildebrandt P, Mroginski MA, Miller AF. Spectroscopic, thermodynamic and computational evidence of the locations of the FADs in the nitrogen fixation-associated electron transfer flavoprotein. Chemical Science. 10: 7762-7772. PMID 31588324 DOI: 10.1039/C9Sc00942F  0.377
2018 Schut GJ, Mohamed-Raseek N, Tokmina-Lukaszewska M, Mulder DW, Nguyen DMN, Lipscomb GL, Hoben JP, Patterson A, Lubner CE, King PW, Peters JW, Bothner B, Miller AF, Adams MWW. The catalytic mechanism of electron bifurcating electron transfer flavoproteins (ETFs) involves an intermediary complex with NAD. The Journal of Biological Chemistry. PMID 30567738 DOI: 10.1074/Jbc.Ra118.005653  0.394
2018 Duan HD, Lubner CE, Tokmina-Lukaszewska M, Gauss GH, Bothner B, King PW, Peters JW, Miller AF. Distinct properties underlie flavin-based electron bifurcation in a novel electron transfer flavoprotein FixAB from. The Journal of Biological Chemistry. PMID 29462786 DOI: 10.1074/Jbc.Ra117.000707  0.334
2018 Miller AF, Park JT, Ferguson KL, Pitsawong W, Bommarius AS. Informing Efforts to Develop Nitroreductase for Amine Production. Molecules (Basel, Switzerland). 23. PMID 29364838 DOI: 10.3390/Molecules23020211  0.369
2017 Miller AF, Wang T. A Single Outer-Sphere Mutation Stabilizes apo-Mn Superoxide Dismutase by 35 °C and Disfavors Mn Binding. Biochemistry. PMID 28704037 DOI: 10.1021/Acs.Biochem.7B00175  0.498
2017 Hoben JP, Lubner CE, Ratzloff MW, Schut GJ, Nguyen DMN, Hempel KW, Adams MWW, King PW, Miller AF. Equilibrium and ultrafast kinetic studies manipulating electron transfer: a short-lived flavin semiquinone is not sufficient for electron bifurcation. The Journal of Biological Chemistry. PMID 28615449 DOI: 10.1074/Jbc.M117.794214  0.316
2017 Pitsawong W, Haynes CA, Koder RL, Rodgers DW, Miller AF. Mechanism-Informed Refinement Reveals Altered Substrate-Binding Mode for Catalytically Competent Nitroreductase. Structure (London, England : 1993). PMID 28578873 DOI: 10.1016/J.Str.2017.05.002  0.34
2014 Miller AF. Solid-state NMR of flavins and flavoproteins. Methods in Molecular Biology (Clifton, N.J.). 1146: 307-40. PMID 24764096 DOI: 10.1007/978-1-4939-0452-5_12  0.356
2014 Pitsawong W, Hoben JP, Miller AF. Understanding the broad substrate repertoire of nitroreductase based on its kinetic mechanism. The Journal of Biological Chemistry. 289: 15203-14. PMID 24706760 DOI: 10.1074/Jbc.M113.547117  0.319
2014 Miller AF, de Paula JC, Brudvig GW. Formation of the S2 state and structure of the Mn complex in photosystem II lacking the extrinsic 33 kilodalton polypeptide. Photosynthesis Research. 12: 205-18. PMID 24435688 DOI: 10.1007/Bf00055121  0.543
2014 Pan J, Bhardwaj M, Faulkner JR, Nagabhyru P, Charlton ND, Higashi RM, Miller AF, Young CA, Grossman RB, Schardl CL. Ether bridge formation in loline alkaloid biosynthesis. Phytochemistry. 98: 60-8. PMID 24374065 DOI: 10.1016/J.Phytochem.2013.11.015  0.335
2013 Jackson TA, Gutman CT, Maliekal J, Miller AF, Brunold TC. Geometric and electronic structures of manganese-substituted iron superoxide dismutase. Inorganic Chemistry. 52: 3356-67. PMID 23461587 DOI: 10.1021/Ic302867Y  0.605
2012 Maly T, Cui D, Griffin RG, Miller AF. 1H dynamic nuclear polarization based on an endogenous radical. The Journal of Physical Chemistry. B. 116: 7055-65. PMID 22472179 DOI: 10.1021/Jp300539J  0.326
2012 Miller AF. Superoxide dismutases: ancient enzymes and new insights. Febs Letters. 586: 585-95. PMID 22079668 DOI: 10.1016/J.Febslet.2011.10.048  0.54
2011 Cui D, Koder RL, Dutton PL, Miller AF. 15N solid-state NMR as a probe of flavin H-bonding. The Journal of Physical Chemistry. B. 115: 7788-98. PMID 21619002 DOI: 10.1021/Jp202138D  0.373
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  0.79
2008 Cerda JF, Koder RL, Lichtenstein BR, Moser CM, Miller AF, Dutton PL. Hydrogen bond-free flavin redox properties: managing flavins in extreme aprotic solvents. Organic & Biomolecular Chemistry. 6: 2204-12. PMID 18528583 DOI: 10.1039/B801952E  0.313
2008 Miller AF. The shortest wire. Proceedings of the National Academy of Sciences of the United States of America. 105: 7341-2. PMID 18508968 DOI: 10.1073/Pnas.0803099105  0.387
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  0.831
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  0.819
2008 Miller AF. Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase. Accounts of Chemical Research. 41: 501-10. PMID 18376853 DOI: 10.1021/Ar700237U  0.545
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  0.74
2007 Koder RL, Lichtenstein BR, Cerda JF, Miller AF, Dutton PL. A Flavin Analogue with Improved Solubility in Organic Solvents. Tetrahedron Letters. 48: 5517-5520. PMID 19568318 DOI: 10.1016/J.Tetlet.2007.05.165  0.303
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  0.824
2006 Koder RL, Walsh JD, Pometun MS, Dutton PL, Wittebort RJ, Miller AF. 15N solid-state NMR provides a sensitive probe of oxidized flavin reactive sites. Journal of the American Chemical Society. 128: 15200-8. PMID 17117871 DOI: 10.1021/Ja0648817  0.363
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  0.813
2005 Miller AF, Sorkin DL, Padmakumar K. Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34. Biochemistry. 44: 5969-81. PMID 15835886 DOI: 10.1021/Bi0476331  0.555
2005 Jackson TA, Karapetian A, Miller AF, Brunold TC. Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of oxidized manganese superoxide dismutase. Biochemistry. 44: 1504-20. PMID 15683235 DOI: 10.1021/Bi048639T  0.339
2004 Jackson TA, Karapetian A, Miller AF, Brunold TC. Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: definitive assignment of the ligand responsible for the low-temperature thermochromism. Journal of the American Chemical Society. 126: 12477-91. PMID 15453782 DOI: 10.1021/Ja0482583  0.398
2004 Miller AF. Superoxide dismutases: active sites that save, but a protein that kills. Current Opinion in Chemical Biology. 8: 162-8. PMID 15062777 DOI: 10.1016/J.Cbpa.2004.02.011  0.474
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  0.812
2003 Miller AF, Padmakumar K, Sorkin DL, Karapetian A, Vance CK. Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase. Journal of Inorganic Biochemistry. 93: 71-83. PMID 12538055 DOI: 10.1016/S0162-0134(02)00621-9  0.46
2003 Walsh JD, Miller A. NMR Shieldings and Electron Correlation Reveal Remarkable Behavior on the Part of the Flavin N5Reactive Center The Journal of Physical Chemistry B. 107: 854-863. DOI: 10.1021/Jp022005J  0.316
2003 Walsh JD, Miller A. Flavin reduction potential tuning by substitution and bending Journal of Molecular Structure: Theochem. 623: 185-195. DOI: 10.1016/S0166-1280(02)00719-4  0.362
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  0.821
2002 Koder RL, Haynes CA, Rodgers ME, Rodgers DW, Miller AF. Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases Biochemistry. 41: 14197-14205. PMID 12450383 DOI: 10.1021/Bi025805T  0.393
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  0.79
2002 Nivinskas H, Staskeviciene S, Sarlauskas J, Koder RL, Miller AF, Cenas N. Two-electron reduction of quinones by Enterobacter cloacae NAD(P)H:nitroreductase: quantitative structure-activity relationships. Archives of Biochemistry and Biophysics. 403: 249-58. PMID 12139974 DOI: 10.1016/S0003-9861(02)00228-X  0.359
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  0.784
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  0.811
2002 Haynes CA, Koder RL, Miller AF, Rodgers DW. Structures of nitroreductase in three states. Effects of inhibitor binding and reduction Journal of Biological Chemistry. 277: 11513-11520. PMID 11805110 DOI: 10.1074/Jbc.M111334200  0.371
2001 Koder RL, Oyedele O, Miller AF. Retro-nitroreductase, a putative evolutionary precursor to Enterobacter cloacae strain 96-3 nitroreductase Antioxidants and Redox Signaling. 3: 747-755. PMID 11761325 DOI: 10.1089/15230860152664957  0.312
2001 Vance CK, Miller AF. Novel insights into the basis for Escherichia coli superoxide dismutase's metal ion specificity from Mn-substituted FeSOD and its very high E(m). Biochemistry. 40: 13079-87. PMID 11669646 DOI: 10.1021/Bi0113317  0.493
2001 Nivinskas H, Koder RL, Anusevičius Z, Šarlauskas J, Miller AF, Čenas N. Quantitative structure-activity relationships in two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H:nitroreductase Archives of Biochemistry and Biophysics. 385: 170-178. PMID 11361014 DOI: 10.1006/Abbi.2000.2127  0.378
2000 Sorkin DL, Miller AF. Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and iron(III)-superoxide dismutase from Escherichia coli Journal of Biomolecular Nmr. 17: 311-322. PMID 11014595 DOI: 10.1023/A:1008344210662  0.534
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  0.796
2000 Vathyam S, Byrd RA, Miller A. Mapping the effects of metal ion reduction and substrate analog binding to Fe-superoxide dismutase by NMR spectroscopy Magnetic Resonance in Chemistry. 38: 536-542. DOI: 10.1002/1097-458X(200007)38:7<536::Aid-Mrc719>3.0.Co;2-8  0.823
1999 Vathyam S, Byrd RA, Miller AF. Assignment of the backbone resonances of oxidized Fe-superoxide dismutase, a 42 kDa paramagnet-containing enzyme. Journal of Biomolecular Nmr. 14: 293-4. PMID 10481283 DOI: 10.1023/A:1008348716066  0.801
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  0.759
1998 Koder RL, Miller AF. Steady-state kinetic mechanism, stereospecificity, substrate and inhibitor specificity of Enterobacter cloacae nitroreductase Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1387: 395-405. PMID 9748656 DOI: 10.1016/S0167-4838(98)00151-4  0.346
1998 Koder RL, Miller AF. Overexpression, isotopic labeling, and spectral characterization of Enterobacter cloacae nitroreductase Protein Expression and Purification. 13: 53-60. PMID 9631515 DOI: 10.1006/Prep.1997.0866  0.385
1998 Vance CK, Miller A. Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase. Biochemistry. 37: 5518-5527. PMID 9548935 DOI: 10.1021/Bi972580R  0.552
1997 Sorkin DL, Duong DK, Miller A. Mutation of Tyrosine 34 to Phenylalanine Eliminates the Active Site pK of Reduced Iron-Containing Superoxide Dismutase † Biochemistry. 36: 8202-8208. PMID 9204864 DOI: 10.1021/Bi970533T  0.577
1997 Sorkin DL, Miller A. Spectroscopic Measurement of a Long-Predicted Active Site pK in Iron-Superoxide Dismutase from Escherichia coli † Biochemistry. 36: 4916-4924. PMID 9125513 DOI: 10.1021/Bi963047Z  0.556
1997 Vance CK, Kang YM, Miller A. Selective 15N labeling and direct observation by NMR of the active-site glutamine of Fe-containing superoxide dismutase. Journal of Biomolecular Nmr. 9: 201-206. PMID 9090133 DOI: 10.1023/A:1018662421878  0.511
1995 Abeygunawardana C, Weber DJ, Gittis AG, Frick DN, Lin J, Miller AF, Bessman MJ, Mildvan AS. Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase. Biochemistry. 34: 14997-5005. PMID 7578113 DOI: 10.1021/Bi00046A006  0.313
1991 Miller AF, Brudvig GW. A guide to electron paramagnetic resonance spectroscopy of Photosystem II membranes. Biochimica Et Biophysica Acta. 1056: 1-18. PMID 1845842 DOI: 10.1016/S0005-2728(05)80067-2  0.498
1988 Thompson LK, Miller A, De Paula JC, Brudvig GW. Electron Donation in Photosystem II Israel Journal of Chemistry. 28: 121-128. DOI: 10.1002/Ijch.198800021  0.593
1987 De Paula JC, Beck WF, Miller AF, Wilson RB, Brudvig GW. Studies of the manganese site of photosystem II by electron spin resonance spectroscopy Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases. 83: 3635-3651. DOI: 10.1039/F19878303635  0.659
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