Susan Miller, PhD

Title(s)Professor Emeritus, Pharmaceutical Chemistry
SchoolSchool of Pharmacy
Address600 16th Street, #S512B
San Francisco CA 94158
ORCID ORCID Icon0000-0002-8221-930X Additional info
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    Collapse Biography 
    Collapse Education and Training
    University of California, BerkeleyPhD1983Chemistry
    University of California, San Francisco2021Diversity, Equity, and Inclusion Champion Training
    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.

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    Identifying Key Proteins In Hg Methylation Pathways of Desulfovibrio by Global Proteomics
    DOE-Office of Science DE-SC0007014Sep 1, 2011 - Sep 14, 2014
    Role: Co-Principal Investigator
    Description: Aims to use global proteomics approach to identify proteins in Desulfovibrio associated with Hg(II) or MeHg upon exposure to Hg(II) in an effort to identify pathways involved in Hg(II) uptake and methylation and release of MeHg into the environment.
    Molecular Mechanisms of Bacterial Mercury Transformation
    DOE Office of Science DE-SC0004919Sep 1, 2010 - Dec 15, 2013
    Role: Co-Principal Investigator
    Description: Computational and mutational studies of catalytic and metal ion transfer mechanisms of enzymes from bacterial mercury resistance pathways.
    Defining the Molecular-Cellular-Field Continuum Of Mercury Detoxification
    DOE Office of Science DE-SC0004735Jun 15, 2010 - Jun 15, 2014
    Role: Co-Principal Investigator
    Description: Structural and functional studies of proteins from different bacterial mercury resistance operons with varied structural features to elucidate their interactions with each other and with the host cell machinery.
    Identifying Biomarkers and Mechanisms of Toxic Metal Stress with Global Proteomics
    DOE-Office of Science DE-FG02-07ER64409May 15, 2007 - May 14, 2011
    Role: Co-Principal Investigator
    Description: Developed a global proteomics approach coupled with a novel computational filter to identify mercury-modified proteins in cells exposed to organomercurials or inorganic mercury.
    Function, Evolution, and Application of the Supramolecular Machines of Hg Detoxification
    DOE-Office of Science DE-FG02-05ER64120Sep 1, 2005 - Aug 31, 2009
    Description: Structure/function studies of interactions between several proteins within the bacterial mercury resistance pathway.
    Engineering MerR for Sequestration and MerA for Reduction of Toxic Metals and Radionuclides (A. Summers
    DE-FG02-99ER62865 RR182-289/5812237Sep 1, 2002 - Aug 31, 2006
    Role: Co-Investigator
    Description: Elucidation and attempted engineering of enzymatic activity of mercuric ion reductase (MerA) towards reduction of toxic metal ions other than mercury.
    Structure/function analysis of protein-protein interactions and role of dynamic motions in mercuric ion reductase
    DOE, Office of Science DE-FG03-01ER63087Jan 15, 2001 - Jan 14, 2005
    Role: Principal Investigator
    Description: Structural, thermodynamic and kinetic analysis of key factors of importance to catalysis and to in vivo efficacy using wild type and mutant forms of the catalytic core and N-terminal domains of mercuric ion reductase
    Structural Control of Hg(II) Transfer and Reduction in Mercuric Ion Reductase
    NSF MCB-9982576Mar 1, 2000 - Feb 28, 2004
    Role: Principal Investigator
    Description: Elucidation of NMR structure and role of N-terminal domain of mercuric ion reductase in Hg(II) substrate binding and transfer to catalytic core
    NIH R29GM050670Jan 1, 1995 - Dec 31, 2000
    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

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    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. to make corrections and additions.
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    Altmetrics Details PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. 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. Kathryn D Bewley, Philip R Bennallack, Mark A Burlingame, Richard A Robison, Joel S Griffitts, Susan M Miller. . View Publication.
    2. Reconstitution and Minimization of a Micrococcin Biosynthetic Pathway in Bacillus subtilis. J Bacteriol. 2016 09 15; 198(18):2431-8. Bennallack PR, Bewley KD, Burlingame MA, Robison RA, Miller SM, Griffitts JS. PMID: 27381911; PMCID: PMC4999933.
      View in: PubMed   Mentions: 10     Fields:    Translation:Cells
    3. 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. Pan S, Sommese RF, Sallam KI, Nag S, Sutton S, Miller SM, Spudich JA, Ruppel KM, Ashley EA. PMID: 26498512; PMCID: PMC4620603.
      View in: PubMed   Mentions: 3     Fields:    Translation:Humans
    4. 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. LaVoie SP, Mapolelo DT, Cowart DM, Polacco BJ, Johnson MK, Scott RA, Miller SM, Summers AO. PMID: 26498643; PMCID: PMC4749482.
      View in: PubMed   Mentions: 5     Fields:    Translation:Cells
    5. 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. Lian P, Guo HB, Riccardi D, Dong A, Parks JM, Xu Q, Pai EF, Miller SM, Wei DQ, Smith JC, Guo H. PMID: 25343681; PMCID: PMC4245977.
      View in: PubMed   Mentions: 14     Fields:    Translation:Cells
    6. Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase. Biophys J. 2014 Jul 15; 107(2):393-400. 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. PMID: 25028881; PMCID: PMC4104034.
      View in: PubMed   Mentions: 5     Fields:    Translation:Cells
    7. Effects of Troponin T Cardiomyopathy Mutations on the Calcium Sensitivity of the Regulated Thin Filament and the Actomyosin Cross-bridge Kinetics of Human β-Cardiac Myosin. Plos One. 2013; (8):e83403. Sommese RF, Nag S, Sutton S, Miller SM, Spudich JA, Ruppel KM.
    8. Why Mercury Prefers Soft Ligands. J. Phys. Chem. Lett. 2013; (4):2317-2322. Riccardi D, Guo H-B, Parks JM, Gu B, Summers AO, Miller SM, Liang L, Smith JC.
    9. 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. Johs A, Harwood IM, Parks JM, Nauss RE, Smith JC, Liang L, Miller SM. PMID: 21893070.
      View in: PubMed   Mentions: 11     Fields:    Translation:Cells
    10. 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. Polacco BJ, Purvine SO, Zink EM, Lavoie SP, Lipton MS, Summers AO, Miller SM. PMID: 21532010; PMCID: PMC3149085.
      View in: PubMed   Mentions: 6     Fields:    Translation:AnimalsCells
    11. 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. Song B, Galande AK, Kodokula K, Moos WH, Miller SM.
    12. 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. Ledwidge R, Hong B, Dötsch V, Miller SM. PMID: 20828160.
      View in: PubMed   Mentions: 9     Fields:    Translation:Cells
    13. Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved γ-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione . Biochemistry. 2010 Sep 21; 49(37):8187-96. Hong B, Nauss R, Harwood IM, Miller SM. PMID: 20722420; PMCID: PMC3042367.
      View in: PubMed   Mentions: 5     Fields:    Translation:Cells
    14. Structure and conformational dynamics of the metalloregulator MerR upon binding of Hg(II). J Mol Biol. 2010 May 14; 398(4):555-68. Guo HB, Johs A, Parks JM, Olliff L, Miller SM, Summers AO, Liang L, Smith JC. PMID: 20303978.
      View in: PubMed   Mentions: 12     Fields:    Translation:Cells
    15. Mechanism of Hg-C protonolysis in the organomercurial lyase MerB. J Am Chem Soc. 2009 Sep 23; 131(37):13278-85. Parks JM, Guo H, Momany C, Liang L, Miller SM, Summers AO, Smith JC. PMID: 19719173.
      View in: PubMed   Mentions: 12     Fields:    Translation:Cells
    16. Kinetic buffering of cross talk between bacterial two-component sensors. J Mol Biol. 2009 Jul 17; 390(3):380-93. Groban ES, Clarke EJ, Salis HM, Miller SM, Voigt CA. PMID: 19445950; PMCID: PMC2974629.
      View in: PubMed   Mentions: 47     Fields:    Translation:Cells
    17. 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. Farady CJ, Sun J, Darragh MR, Miller SM, Craik CS. PMID: 17475279; PMCID: PMC2041882.
      View in: PubMed   Mentions: 24     Fields:    Translation:HumansAnimalsCells
    18. 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. Ledwidge R, Patel B, Dong A, Fiedler D, Falkowski M, Zelikova J, Summers AO, Pai EF, Miller SM. PMID: 16114877.
      View in: PubMed   Mentions: 29     Fields:    Translation:HumansCells
    19. Direct monitoring of metal ion transfer between two trafficking proteins. J Am Chem Soc. 2005 Aug 10; 127(31):10842-3. Ledwidge R, Soinski R, Miller SM. PMID: 16076185.
      View in: PubMed   Mentions: 2     Fields:    
    20. Mercury adaptation among bacteria from a deep-sea hydrothermal vent. Appl Environ Microbiol. 2005 Jan; 71(1):220-6. Vetriani C, Chew YS, Miller SM, Yagi J, Coombs J, Lutz RA, Barkay T. PMID: 15640191; PMCID: PMC544242.
      View in: PubMed   Mentions: 34     Fields:    Translation:Cells
    21. Quantitative identification of the protonation state of histidines in vitro and in vivo. Biochemistry. 2003 Aug 05; 42(30):9227-34. Shimba N, Serber Z, Ledwidge R, Miller SM, Craik CS, Dötsch V. PMID: 12885258.
      View in: PubMed   Mentions: 18     Fields:    Translation:Cells
    22. Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol Rev. 2003 Jun; 27(2-3):355-84. Barkay T, Miller SM, Summers AO. PMID: 12829275.
      View in: PubMed   Mentions: 198     Fields:    Translation:CellsPHPublic Health
    23. 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. Serber Z, Ledwidge R, Miller SM, Dötsch V. PMID: 11552796.
      View in: PubMed   Mentions: 37     Fields:    Translation:HumansCells
    24. High-resolution macromolecular NMR spectroscopy inside living cells. J Am Chem Soc. 2001 Mar 14; 123(10):2446-7. Serber Z, Keatinge-Clay AT, Ledwidge R, Kelly AE, Miller SM, Dötsch V. PMID: 11456903.
      View in: PubMed   Mentions: 47     Fields:    
    25. 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. Buckman J, Miller SM. PMID: 10956043.
      View in: PubMed   Mentions: 1     Fields:    Translation:AnimalsCells
    26. 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. Buckman J, Miller SM. PMID: 10956044.
      View in: PubMed   Mentions: 1     Fields:    Translation:AnimalsCells
    27. No metal cofactor in orotidine 5'-monophosphate decarboxylase. Biochem Biophys Res Commun. 1999 May 27; 259(1):133-5. Cui W, DeWitt JG, Miller SM, Wu W. PMID: 10334928.
      View in: PubMed   Mentions: 7     Fields:    Translation:AnimalsCells
    28. 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. Samuels NM, Gibson BW, Miller SM. PMID: 10320348.
      View in: PubMed   Mentions: 4     Fields:    Translation:Cells
    29. 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. Engst S, Miller SM. PMID: 10090738.
      View in: PubMed   Mentions: 11     Fields:    Translation:Cells
    30. Bacterial detoxification of Hg(II) and organomercurials. Essays Biochem. 1999; 34:17-30. Miller SM. PMID: 10730186.
      View in: PubMed   Mentions: 9     Fields:    Translation:Cells
    31. Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates. Biochemistry. 1998 Oct 06; 37(40):14326-36. Buckman J, Miller SM. PMID: 9760270.
      View in: PubMed   Mentions: 8     Fields:    Translation:AnimalsCells
    32. 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. Engst S, Miller SM. PMID: 9708985.
      View in: PubMed   Mentions: 8     Fields:    Translation:Cells
    33. Bioorg & Med Chem Lett. Decarboxylation of 1,3- Dimethylorotic Acid Revisited: Determining the Role of N-1. 1997; 7:2623-2628. Wu W, Ley-han A, Wong FM, Austin TJ, Miller SM.
    34. 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. Miller SM. PMID: 7548066.
      View in: PubMed   Mentions:    Fields:    Translation:Cells
    35. 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. Miller SM, Simon RJ, Ng S, Zuckermann, RN, Kerr JM, Moos WH.
    36. Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme. J Biol Chem. 1994 Jan 07; 269(1):150-5. Arunachalam U, Massey V, Miller SM. PMID: 8276789.
      View in: PubMed   Mentions: 11     Fields:    Translation:Cells
    37. Bioorg & Med Chem Letters. Proteolytic Studies of Homologous Peptide and N-Substituted Glycine Peptoid Oligomers. 1994; 4:2657-2662. Miller SM, Simon RJ, Ng S, Zuckermann RN, Kerr JM, Moos WH.
    38. C-terminal cysteines of Tn501 mercuric ion reductase. Biochemistry. 1992 Feb 18; 31(6):1677-85. Moore MJ, Miller SM, Walsh CT. PMID: 1531297.
      View in: PubMed   Mentions: 10     Fields:    Translation:Cells
    39. Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis. Biochemistry. 1991 Mar 12; 30(10):2600-12. Miller SM, Massey V, Williams CH, Ballou DP, Walsh CT. PMID: 2001350.
      View in: PubMed   Mentions: 10     Fields:    Translation:Cells
    40. 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. Miller SM, Massey V, Ballou D, Williams CH, Distefano MD, Moore MJ, Walsh CT. PMID: 2189497.
      View in: PubMed   Mentions: 23     Fields:    Translation:Cells
    41. Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry. 1989 Feb 07; 28(3):1194-205. Miller SM, Moore MJ, Massey V, Williams CH, Distefano MD, Ballou DP, Walsh CT. PMID: 2653437.
      View in: PubMed   Mentions: 19     Fields:    Translation:Cells
    42. 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. Miller SM, Ballou DP, Massey V, Williams CH, Walsh CT. PMID: 3522563.
      View in: PubMed   Mentions: 4     Fields:    Translation:Cells
    43. 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. Miller SM, Klinman JP. PMID: 3995006.
      View in: PubMed   Mentions: 13     Fields:    
    44. Magnitude of intrinsic isotope effects in the dopamine beta-monooxygenase reaction. Biochemistry. 1983 Jun 21; 22(13):3091-6. Miller SM, Klinman JP. PMID: 6882738.
      View in: PubMed   Mentions: 10     Fields:    Translation:Animals
    45. Deduction of kinetic mechanisms from primary hydrogen isotope effects: dopamine beta-monooxygenase--a case history. Methods Enzymol. 1982; 87:711-32. Miller SM, Klinman JP. PMID: 7176929.
      View in: PubMed   Mentions: 2     Fields:    
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