Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation

Proc Natl Acad Sci USA. 2016 Nov 1;113(44):12450-12455.

Kathryn D Bewley, Philip R Bennallack, Mark A Burlingame, Richard A Robison, Joel S Griffitts, Susan M Miller

Reconstitution and Minimization of a Micrococcin Biosynthetic Pathway in Bacillus subtilis.

Journal of bacteriology. 2016 July 5.

Bennallack PR, Bewley KD, Burlingame MA, Robison RA, Miller SM, Griffitts JS


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 medical genetics. 2015 Oct 26;16:97.

Pan S, Sommese RF, Sallam KI, Nag S, Sutton S, Miller SM, Spudich JA, Ruppel KM, Ashley EA

Organic and inorganic mercurials have distinct effects on cellular thiols, metal homeostasis, and Fe-binding proteins in Escherichia coli.

Journal of biological inorganic chemistry. 2015 Dec;20(8):1239-51.

LaVoie SP, Mapolelo DT, Cowart DM, Polacco BJ, Johnson MK, Scott RA, Miller SM, Summers AO


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):7211-7222.

Lian P, Guo HB, Riccardi D, Dong A, Parks JM, Xu Q, Pai EF, Miller SM, Wei DQ, Smith JC, Guo H

Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase.

Biophysical journal. 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


Why Mercury Prefers Soft Ligands

J. Phys. Chem. Lett. 2013 Jun 27;4(14):2317-2322

Riccardi D, Guo H-B, Parks JM, Gu B, Summers AO, Miller SM, Liang L, Smith JC.

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(12).

Sommese RF, Nag S, Sutton S, Miller SM, Spudich JA, Ruppel KM


Structural characterization of intramolecular Hg(2+) transfer between flexibly linked domains of mercuric ion reductase.

Journal of Molecular Biology. 2011 Oct 28;413(3):639-56

Johs A, Harwood IM, Parks JM, Nauss RE, Smith JC, Liang L, Miller SM

Discovering mercury protein modifications in whole proteomes using natural isotope distributions observed in liquid chromatography-tandem mass spectrometry.

Molecular & Cellular Proteomics : MCP. 2011 Aug;10(8):M110.004853.

Polacco BJ, Purvine SO, Zink EM, Lavoie SP, Lipton MS, Summers AO, 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

Ledwidge R, Hong B, Dötsch V, 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.

Hong B, Nauss R, Harwood IM, Miller SM

Structure and conformational dynamics of the metalloregulator MerR upon binding of Hg(II).

Journal of Molecular Biology. 2011 Oct 28;413(3):639-56.

Guo HB, Johs A, Parks JM, Olliff L, Miller SM, Summers AO, Liang L, Smith JC


Mechanism of Hg-C protonolysis in the organomercurial lyase MerB.

Journal of the American Chemical Society. 2009 Sep 23;131(37):13278-85.

Parks JM, Guo H, Momany C, Liang L, Miller SM, Summers AO, Smith JC

Kinetic buffering of cross talk between bacterial two-component sensors.

Journal of Molecular Biology. 2009 Jul 17;390(3):380-93.

Groban ES, Clarke EJ, Salis HM, Miller SM, Voigt CA


The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1).

Journal of Molecular Biology. 2007 Jun 15;369(4):1041-51.

Farady CJ, Sun J, Darragh MR, Miller SM, Craik CS


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

Direct monitoring of metal ion transfer between two trafficking proteins.

Journal of the American Chemical Society. 2005 Aug 10;127(31):10842-3.

Ledwidge R, Soinski R, Miller SM

Mercury adaptation among bacteria from a deep-sea hydrothermal vent.

Applied and Environmental Microbiology. 2005 Jan; 71(1): 220–226.

Vetriani C, Chew YS, Miller SM, Yagi J, Coombs J, Lutz RA, Barkay T


Quantitative identification of the protonation state of histidines in vitro and in vivo.

Biochemistry. 2003 Aug 5;42(30):9227-34.

Shimba N, Serber Z, Ledwidge R, Miller SM, Craik CS, Dötsch V

Bacterial mercury resistance from atoms to ecosystems.

FEMS Microbiology Reviews. 2003 Jun;27(2-3):355-84.

Barkay T, Miller SM, Summers AO


Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy.

Journal of the American Chemical Society. 2001 Sep 19;123(37):8895-901.

Serber Z, Ledwidge R, Miller SM, Dötsch V

High-resolution macromolecular NMR spectroscopy inside living cells.

Journal of the American Chemical Society. 2001 Mar 14;123(10):2446-7.

Serber Z, Keatinge-Clay AT, Ledwidge R, Kelly AE, Miller SM, Dötsch V


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

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


No metal cofactor in orotidine 5'-monophosphate decarboxylase.

Biochemical and Biophysical Research Communications. 1999 May 27;259(1):133-5.

Cui W, DeWitt JG, Miller SM, Wu W

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

Alternative routes for entry of HgX2 into the active site of mercuric ion reductase depend on the nature of the X ligands.

Biochemistry. Mar 23;38(12):3519-29.

Engst S, Miller SM

Bacterial detoxification of Hg(II) and organomercurials.

Essays in Biochemistry. 1999;34:17-30.

Miller SM


Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates.

Biochemistry. 1998 Oct 6;37(40):14326-36.

Buckman J, 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.

Engst S, Miller SM

Decarboxylation of 1,3- Dimethylorotic Acid Revisited: Determining the Role of N-1

Bioorg & Med Chem Lett. 

Wu W, Ley-han A, Wong FM, Austin TJ, 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.


Miller SM

Drug Dev Res

Comparison of the Proteolytic Susceptabilities of Homologous L-Amino Acid, D-Amino Acid, and NSubstituted Glycine Peptide and Peptoid Oligomers

Miller SM, Simon RJ, Ng S, Zuckermann, RN, Kerr JM, Moos WH

Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme.

The Journal of biological chemistry

Arunachalam U, Massey V, Miller SM

Bioorg & Med Chem Letters

Proteolytic Studies of Homologous Peptide and N-Substituted Glycine Peptoid Oligomers

Miller SM, Simon RJ, Ng S, Zuckermann RN, Kerr JM, Moos WH

C-terminal cysteines of Tn501 mercuric ion reductase.


Moore MJ, Miller SM, Walsh CT

Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis.


Miller SM, Massey V, Williams CH, Ballou DP, 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.


Miller SM, Massey V, Ballou D, Williams CH, Distefano MD, Moore MJ, Walsh CT

Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase.


Miller SM, Moore MJ, Massey V, Williams CH, Distefano MD, Ballou DP, Walsh CT

Two-electron reduced mercuric reductase binds Hg(II) to the active site dithiol but does not catalyze Hg(II) reduction.

The Journal of biological chemistry

Miller SM, Ballou DP, Massey V, Williams CH, Walsh CT

Secondary isotope effects and structure-reactivity correlations in the dopamine beta-monooxygenase reaction: evidence for a chemical mechanism.


Miller SM, Klinman JP

Magnitude of intrinsic isotope effects in the dopamine beta-monooxygenase reaction.


Miller SM, Klinman JP

Deduction of kinetic mechanisms from primary hydrogen isotope effects: dopamine beta-monooxygenase--a case history.

Methods in enzymology

Miller SM, Klinman JP