Susan Miller, PhD

SchoolUCSF School of Pharmacy
DepartmentPharmaceutical Chemistry
Address600 16th St
San Francisco CA 94158
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    Collapse Biography 
    Collapse Awards and Honors
    1974National Merit Scholar
    University of Missouri 1974Curator's Scholar Award
    University of Missouri1977Phi Lambda Upsilon
    University of Missouri1978Phi Beta Kappa
    University of California1984Sigma Xi

    Collapse Overview 
    Collapse Overview
    Broadly, we use a variety of biochemical and biophysical tools to investigate protein structure/function questions spanning the range of elucidating novel aspects of catalysis in individual enzymes to understanding the interactions of proteins within a pathway and how mutations influence flux through the pathway. Current work is focused on understanding how key enzymes and transport proteins of bacterial mercury detoxification pathways work individually, with each other, and with other host cell proteins to rapidly remove the toxic threat of organomercurials (such as Methyl-Hg) and mercuric ions from their environment.

    Collapse Research 
    Collapse Research Activities and Funding
    NIH/NIGMS R29GM050670Jan 1, 1995 - Dec 31, 2000
    Role: Principal Investigator
    HRSA/BHP D31AH055008Oct 1, 1990 - Sep 30, 1993
    Role: Principal Investigator
    Bio-Organic Biomedical Mass Spectrometry Resource
    NIH P41RR001614Mar 1, 1982 - May 31, 2015
    Role: Co-Investigator
    Resource for Biocomputing, Visualization, and Informatics
    NIH/NCRR P41RR001081Jun 1, 1976 - Sep 14, 2012
    Role: Co-Investigator

    Collapse ORNG Applications 
    Collapse Websites
    Collapse Global Health

    Collapse Bibliographic 
    Collapse Publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Researchers can login to make corrections and additions, or contact us for help.
    List All   |   Timeline
    1. Kathryn D Bewley, Philip R Bennallack, Mark A Burlingame, Richard A Robison, Joel S Griffitts, Susan M Miller. Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation. Proc Natl Acad Sci USA. 2016; 113(44):12450-12455.
    2. Bennallack PR, Bewley KD, Burlingame MA, Robison RA, Miller S, Griffitts JS. Reconstitution and Minimization of a Micrococcin Biosynthetic Pathway in Bacillus subtilis. J Bacteriol. 2016 Sep 15; 198(18):2431-8. PMID: 27381911; PMCID: PMC4999933 [Available on 03/15/17].
    3. Pan S, Sommese RF, Sallam KI, Nag S, Sutton S, Miller SM, Spudich JA, Ruppel KM, Ashley EA. Establishing disease causality for a novel gene variant in familial dilated cardiomyopathy using a functional in-vitro assay of regulated thin filaments and human cardiac myosin. BMC Med Genet. 2015 Oct 26; 16:97. PMID: 26498512; PMCID: PMC4620603.
    4. LaVoie SP, Mapolelo DT, Cowart DM, Polacco BJ, Johnson MK, Scott RA, Miller S, Summers AO. Organic and inorganic mercurials have distinct effects on cellular thiols, metal homeostasis, and Fe-binding proteins in Escherichia coli. J Biol Inorg Chem. 2015 Dec; 20(8):1239-51. PMID: 26498643; PMCID: PMC4749482 [Available on 12/01/16].
    5. Lian P, Guo HB, Riccardi D, Dong A, Parks JM, Xu Q, Pai EF, Miller SM, Wei DQ, Smith JC, Guo H. X-ray structure of a Hg2+ complex of mercuric reductase (MerA) and quantum mechanical/molecular mechanical study of Hg2+ transfer between the C-terminal and buried catalytic site cysteine pairs. Biochemistry. 2014 Nov 25; 53(46):7211-22. PMID: 25343681; PMCID: PMC4245977.
    6. Hong L, Sharp MA, Poblete S, Biehl R, Zamponi M, Szekely N, Appavou MS, Winkler RG, Nauss RE, Johs A, Parks JM, Yi Z, Cheng X, Liang L, Ohl M, Miller SM, Richter D, Gompper G, Smith JC. Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase. Biophys J. 2014 Jul 15; 107(2):393-400. PMID: 25028881; PMCID: PMC4104034.
    7. Riccardi D, Guo H-B, Parks JM, Gu B, Summers AO, Miller S, Liang L, Smith JC. Why Mercury Prefers Soft Ligands. J. Phys. Chem. Lett. 2013; (4):2317-2322.
    8. Sommese RF, Nag S, Sutton S, Miller S, Spudich JA, Ruppel KM. Effects of Troponin T Cardiomyopathy Mutations on the Calcium Sensitivity of the Regulated Thin Filament and the Actomyosin Cross-bridge Kinetics of Human ß-Cardiac Myosin. Plos One. 2013; (8):e83403.
    9. Johs A, Harwood IM, Parks JM, Nauss RE, Smith JC, Liang L, Miller SM. Structural characterization of intramolecular Hg(2+) transfer between flexibly linked domains of mercuric ion reductase. J Mol Biol. 2011 Oct 28; 413(3):639-56. PMID: 21893070.
      View in: PubMed
    10. Polacco BJ, Purvine SO, Zink EM, Lavoie SP, Lipton MS, Summers AO, Miller SM. Discovering mercury protein modifications in whole proteomes using natural isotope distributions observed in liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics. 2011 Aug; 10(8):M110.004853. PMID: 21532010; PMCID: PMC3149085.
    11. Song B, Galande AK, Kodokula K, Moos WH, Miller S . Drug Development Research. Evaluation of the pKa Values and Ionization Sequence of Bumetanide in Water Using 1H and 13C NMR and UV Spectroscopy. 2011; 72:1-11.
    12. Ledwidge R, Hong B, Dötsch V, Miller SM. NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols. Biochemistry. 2010 Oct 19; 49(41):8988-98. PMID: 20828160.
      View in: PubMed
    13. Hong B, Nauss R, Harwood IM, Miller SM. Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved ?-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione . Biochemistry. 2010 Sep 21; 49(37):8187-96. PMID: 20722420; PMCID: PMC3042367.
    14. Guo HB, Johs A, Parks JM, Olliff L, Miller SM, Summers AO, Liang L, Smith JC. Structure and conformational dynamics of the metalloregulator MerR upon binding of Hg(II). J Mol Biol. 2010 May 14; 398(4):555-68. PMID: 20303978.
      View in: PubMed
    15. Parks JM, Guo H, Momany C, Liang L, Miller SM, Summers AO, Smith JC. Mechanism of Hg-C protonolysis in the organomercurial lyase MerB. J Am Chem Soc. 2009 Sep 23; 131(37):13278-85. PMID: 19719173.
      View in: PubMed
    16. Groban ES, Clarke EJ, Salis HM, Miller SM, Voigt CA. Kinetic buffering of cross talk between bacterial two-component sensors. J Mol Biol. 2009 Jul 17; 390(3):380-93. PMID: 19445950; PMCID: PMC2974629.
    17. Farady CJ, Sun J, Darragh MR, Miller SM, Craik CS. The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1). J Mol Biol. 2007 Jun 15; 369(4):1041-51. PMID: 17475279; PMCID: PMC2041882.
    18. Ledwidge R, Patel B, Dong A, Fiedler D, Falkowski M, Zelikova J, Summers AO, Pai EF, Miller SM. NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions. Biochemistry. 2005 Aug 30; 44(34):11402-16. PMID: 16114877.
      View in: PubMed
    19. Ledwidge R, Soinski R, Miller SM. Direct monitoring of metal ion transfer between two trafficking proteins. J Am Chem Soc. 2005 Aug 10; 127(31):10842-3. PMID: 16076185.
      View in: PubMed
    20. Vetriani C, Chew YS, Miller SM, Yagi J, Coombs J, Lutz RA, Barkay T. Mercury adaptation among bacteria from a deep-sea hydrothermal vent. Appl Environ Microbiol. 2005 Jan; 71(1):220-6. PMID: 15640191; PMCID: PMC544242.
    21. Shimba N, Serber Z, Ledwidge R, Miller SM, Craik CS, Dötsch V. Quantitative identification of the protonation state of histidines in vitro and in vivo. Biochemistry. 2003 Aug 05; 42(30):9227-34. PMID: 12885258.
      View in: PubMed
    22. Barkay T, Miller SM, Summers AO. Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol Rev. 2003 Jun; 27(2-3):355-84. PMID: 12829275.
      View in: PubMed
    23. Serber Z, Ledwidge R, Miller SM, Dötsch V. Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy. J Am Chem Soc. 2001 Sep 19; 123(37):8895-901. PMID: 11552796.
      View in: PubMed
    24. Serber Z, Keatinge-Clay AT, Ledwidge R, Kelly AE, Miller SM, Dötsch V. High-resolution macromolecular NMR spectroscopy inside living cells. J Am Chem Soc. 2001 Mar 14; 123(10):2446-7. PMID: 11456903.
      View in: PubMed
    25. Buckman J, Miller SM. Transient kinetics and intermediates formed during the electron transfer reaction catalyzed by Candida albicans estrogen binding protein. Biochemistry. 2000 Aug 29; 39(34):10521-31. PMID: 10956043.
      View in: PubMed
    26. Buckman J, Miller SM. Stabilization of a novel enzyme.substrate intermediate in the Y206F mutant of Candida albicans EBP1: evidence for acid catalysis. Biochemistry. 2000 Aug 29; 39(34):10532-41. PMID: 10956044.
      View in: PubMed
    27. Cui W, DeWitt JG, Miller SM, Wu W. No metal cofactor in orotidine 5'-monophosphate decarboxylase. Biochem Biophys Res Commun. 1999 May 27; 259(1):133-5. PMID: 10334928.
      View in: PubMed
    28. Samuels NM, Gibson BW, Miller SM. Investigation of the kinetic mechanism of cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi with new insights on rate-limiting steps from product inhibition analysis. Biochemistry. 1999 May 11; 38(19):6195-203. PMID: 10320348.
      View in: PubMed
    29. Engst S, Miller SM. Alternative routes for entry of HgX2 into the active site of mercuric ion reductase depend on the nature of the X ligands. Biochemistry. 1999 Mar 23; 38(12):3519-29. PMID: 10090738.
      View in: PubMed
    30. Miller SM. Bacterial detoxification of Hg(II) and organomercurials. Essays Biochem. 1999; 34:17-30. PMID: 10730186.
      View in: PubMed
    31. Buckman J, Miller SM. Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates. Biochemistry. 1998 Oct 06; 37(40):14326-36. PMID: 9760270.
      View in: PubMed
    32. Engst S, Miller SM. Rapid reduction of Hg(II) by mercuric ion reductase does not require the conserved C-terminal cysteine pair using HgBr2 as the substrate. Biochemistry. 1998 Aug 18; 37(33):11496-507. PMID: 9708985.
      View in: PubMed
    33. Wu W, Ley-han A, Wong FM, Austin TJ, Miller S . Bioorg & Med Chem Lett. Decarboxylation of 1,3- Dimethylorotic Acid Revisited: Determining the Role of N-1. 1997; 7:2623-2628.
    34. Miller SM. 2'-fluoro-2'-deoxy-D-arabinoflavin: characterization of a novel flavin and its effects on the formation and stability of two-electron-reduced mercuric ion reductase. Biochemistry. 1995 Oct 10; 34(40):13066-73. PMID: 7548066.
      View in: PubMed
    35. Miller S, Simon RJ, Ng S, Zuckermann, RN, Kerr JM, Moos WH. Drug Dev Res. Comparison of the Proteolytic Susceptabilities of Homologous L-Amino Acid, D-Amino Acid, and NSubstituted Glycine Peptide and Peptoid Oligomers. 1995; 35:20-32.
    36. Arunachalam U, Massey V, Miller SM. Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme. J Biol Chem. 1994 Jan 07; 269(1):150-5. PMID: 8276789.
      View in: PubMed
    37. Miller S, Simon RJ, Ng S, Zuckermann RN, Kerr JM, Moos WH. Bioorg & Med Chem Letters. Proteolytic Studies of Homologous Peptide and N-Substituted Glycine Peptoid Oligomers. 1994; 4:2657-2662.
    38. Moore MJ, Miller SM, Walsh CT. C-terminal cysteines of Tn501 mercuric ion reductase. Biochemistry. 1992 Feb 18; 31(6):1677-85. PMID: 1531297.
      View in: PubMed
    39. Miller SM, Massey V, Williams CH, Ballou DP, Walsh CT. Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis. Biochemistry. 1991 Mar 12; 30(10):2600-12. PMID: 2001350.
      View in: PubMed
    40. Miller SM, Massey V, Ballou D, Williams CH, Distefano MD, Moore MJ, Walsh CT. Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase. Biochemistry. 1990 Mar 20; 29(11):2831-41. PMID: 2189497.
      View in: PubMed
    41. Miller SM, Moore MJ, Massey V, Williams CH, Distefano MD, Ballou DP, Walsh CT. Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry. 1989 Feb 07; 28(3):1194-205. PMID: 2653437.
      View in: PubMed
    42. Miller SM, Ballou DP, Massey V, Williams CH, Walsh CT. Two-electron reduced mercuric reductase binds Hg(II) to the active site dithiol but does not catalyze Hg(II) reduction. J Biol Chem. 1986 Jun 25; 261(18):8081-4. PMID: 3522563.
      View in: PubMed
    43. Miller SM, Klinman JP. Secondary isotope effects and structure-reactivity correlations in the dopamine beta-monooxygenase reaction: evidence for a chemical mechanism. Biochemistry. 1985 Apr 23; 24(9):2114-27. PMID: 3995006.
      View in: PubMed
    44. Miller SM, Klinman JP. Magnitude of intrinsic isotope effects in the dopamine beta-monooxygenase reaction. Biochemistry. 1983 Jun 21; 22(13):3091-6. PMID: 6882738.
      View in: PubMed
    45. Miller SM, Klinman JP. Deduction of kinetic mechanisms from primary hydrogen isotope effects: dopamine beta-monooxygenase--a case history. Methods Enzymol. 1982; 87:711-32. PMID: 7176929.
      View in: PubMed
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