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

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

Proc Natl Acad Sci USA. 2016 Oct 17.

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

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

J Bacteriology. 2016 July 5.


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

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

J Biol Inorg Chem. 2015 Dec;20(8):1239-51.

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.

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

BMC Med Genet. 2015 Oct 26;16:97.


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.

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

Biochemistry 2014 Nov 25;53(46):7211-7222.

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

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, Phl M, Miller SM, Richter D, Gompper G, Smith JC.

Biophys J. 2014 Jul 15;107(2):393-400.


Effects of Troponin T Cadiomyophathy Mutations on the Calcium Sensitivity of the Regulated Thin Filament and the Actomyosin Cross-Bridge Kinetics of Human B-Cardiac Myosin.

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

PLoS One. 2013;8(12).

Why Mercury Prefers Soft Ligands.

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

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


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

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

J Mol Biol. 2011 Oct 28;413(3):639-56

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

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

Mol Cell Proteomics. 2011 Aug;10(8):M110.004853.


NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols.

Ledwidge R, Hong B, Dötsch V, Miller SM.

Biochemistry. 2010 Oct 19;49(41):8988-98

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.

Hong B, Nauss R, Harwood IM, Miller SM.

Biochemistry. 2010 Sep 21;49(37):8187-96.


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

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

J Am Chem Soc. 2009 Sep 23;131(37):13278-85.

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

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

J Mol Biol. 2009 Jul 17;390(3):380-93.


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

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

J Mol Biol. 2007 Jun 15;369(4):1041-51.


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.

Ledwidge R, Patel B, Dong A, Fiedler D, Falkowski M, Zelikova J, Summers AO, Pai EF, Miller SM.

Biochemistry. 2005 Aug 30;44(34):11402-16

Direct monitoring of metal ion transfer between two trafficking proteins.

Ledwidge R, Soinski R, Miller SM.

J Am Chem Soc. 2005 Aug 10;127(31):10842-3.


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

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

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

Bacterial mercury resistance from atoms to ecosystems.

Barkay T, Miller SM, Summers AO.

FEMS Microbiol Rev. 2003 Jun;27(2-3):355-84. Review.


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

Serber Z, Ledwidge R, Miller SM, Dötsch V.

J Am Chem Soc. 2001 Sep 19;123(37):8895-901.

High-resolution macromolecular NMR spectroscopy inside living cells.

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

J Am Chem Soc. 2001 Mar 14;123(10):2446-7.


Transient kinetics and intermediates formed during the electron transfer reaction catalyzed by Candida albicans estrogen binding protein.

Buckman J, Miller SM.

Biochemistry. 2000 Aug 29;39(34):10521-31.

Stabilization of a novel enzyme.substrate intermediate in the Y206F mutant of Candida albicans EBP1: evidence for acid catalysis.

Buckman J, Miller SM.

Biochemistry. 2000 Aug 29;39(34):10532-41.


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

Engst S, Miller SM.

Biochemistry. 1999 Mar 23;38(12):3519-29.

Bacterial detoxification of Hg(II) and organomercurials.

Miller SM.

Essays Biochem. 1999;34:17-30. Review.

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.

Samuels NM, Gibson BW, Miller SM.

Biochemistry. 1999 May 11;38(19):6195-203.


Rapid reduction of Hg(II) by mercuric ion reductase does not require the conserved C-terminal cysteine pair using HgBr2 as the substrate.

Engst S, Miller SM.

Biochemistry. 1998 Aug 18;37(33):11496-507.

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

Buckman J, Miller SM.

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


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.

Biochemistry. 1995 Oct 10;34(40):13066-73.


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

Arunachalam U, Massey V, Miller SM.

J Biol Chem. 1994 Jan 7;269(1):150-5.


C-terminal cysteines of Tn501 mercuric ion reductase.

Moore MJ, Miller SM, Walsh CT.

Biochemistry. 1992 Feb 18;31(6):1677-85.


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

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

Biochemistry. 1991 Mar 12;30(10):2600-12.


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 Jr, Distefano MD, Moore MJ, Walsh CT.

Biochemistry. 1990 Mar 20;29(11):2831-41.


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

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

Biochemistry. 1989 Feb 7;28(3):1194-205.


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

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

J Biol Chem. 1986 Jun 25;261(18):8081-4.


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

Miller SM, Klinman JP.

Biochemistry. 1985 Apr 23;24(9):2114-27.


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

Miller SM, Klinman JP.

Biochemistry. 1983 Jun 21;22(13):3091-6.


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

Miller SM, Klinman JP.

Methods Enzymol. 1982;87:711-32.