Sooim Shin

Sooim Shin

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Sooim Shin

Sooim Shin

Publications by authors named "Sooim Shin"

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18Publications

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Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self-cleavage exhibits enhanced enzymatic activity.

FEBS Open Bio 2020 Mar 3. Epub 2020 Mar 3.

Department of Optometry, College of Energy and Biotechnology, Seoul National University of Science and Technology, South Korea.

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http://dx.doi.org/10.1002/2211-5463.12828DOI Listing
March 2020

Copper-binding energetics of amicyanin in different folding states.

Metallomics 2020 Feb 12;12(2):273-279. Epub 2019 Dec 12.

Interdisciplinary Program of Bioenergy and Biomaterials Graduate School, College of Engineering, Chonnam National University, Gwangju 61186, Republic of Korea.

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http://dx.doi.org/10.1039/c9mt00261hDOI Listing
February 2020

Bottom-line mechanism of organochlorine pesticides on mitochondria dysfunction linked with type 2 diabetes.

J Hazard Mater 2020 Feb 25;393:122400. Epub 2020 Feb 25.

Interdisciplinary Program of Bioenergy and Biomaterials Graduate School, College of Engineering, Chonnam National University, Gwangju, 61186, Republic of Korea; Department of Biotechnology and Bioengineering, College of Engineering, Chonnam National University, Gwangju, 61186, Republic of Korea. Electronic address:

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http://dx.doi.org/10.1016/j.jhazmat.2020.122400DOI Listing
February 2020

The action of low doses of persistent organic pollutants (POPs) on mitochondrial function in zebrafish eyes and comparison with hyperglycemia to identify a link between POPs and diabetes.

Toxicol Mech Methods 2020 Jan 28:1-9. Epub 2020 Jan 28.

Interdisciplinary Program of Bioenergy and Biomaterials Graduate School, College of Engineering, Chonnam National University, Gwangju, Republic of Korea.

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http://dx.doi.org/10.1080/15376516.2020.1717704DOI Listing
January 2020

A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.

Biochim Biophys Acta 2015 Aug 17;1847(8):709-16. Epub 2015 Apr 17.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL 32827, USA. Electronic address:

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http://dx.doi.org/10.1016/j.bbabio.2015.04.008DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4458201PMC
August 2015

A simple method to engineer a protein-derived redox cofactor for catalysis.

Biochim Biophys Acta 2014 Oct 22;1837(10):1595-601. Epub 2014 May 22.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL 32827, USA. Electronic address:

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http://dx.doi.org/10.1016/j.bbabio.2014.05.354DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285715PMC
October 2014

Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase.

FEBS Lett 2014 Mar 23;588(5):752-6. Epub 2014 Jan 23.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL 32827, United States. Electronic address:

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http://dx.doi.org/10.1016/j.febslet.2014.01.021DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3972763PMC
March 2014

Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.

Biochemistry 2014 Mar 19;53(8):1342-9. Epub 2014 Feb 19.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida , Orlando, Florida 32827, United States.

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http://pubs.acs.org/doi/10.1021/bi5000349
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http://dx.doi.org/10.1021/bi5000349DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985960PMC
March 2014

MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.

Arch Biochem Biophys 2014 Feb 19;544:112-8. Epub 2013 Oct 19.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL 32827, USA. Electronic address:

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http://dx.doi.org/10.1016/j.abb.2013.10.004DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3946517PMC
February 2014

Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis.

Biochem J 2013 Nov;456(1):129-37

*College of Medicine, Burnett School of Biomedical Sciences, 6900 Lake Nona Boulevard, Orlando, FL 32827, U.S.A.

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http://dx.doi.org/10.1042/BJ20130981DOI Listing
November 2013

Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.

Biochemistry 2013 Sep 30;52(37):6358-67. Epub 2013 Aug 30.

Biochemistry and Physiology Department, College of Medicine, The University of Jordan , Amman, Jordan 11942.

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http://dx.doi.org/10.1021/bi400905sDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901365PMC
September 2013

Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.

FEBS Lett 2012 Dec 2;586(24):4339-43. Epub 2012 Nov 2.

Biochemistry and Physiology Department, College of Medicine, The University of Jordan, Amman 11942, Jordan.

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http://doi.wiley.com/10.1016/j.febslet.2012.10.044
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http://dx.doi.org/10.1016/j.febslet.2012.10.044DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3652260PMC
December 2012

Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex.

Biochemistry 2012 Sep 23;51(35):6942-9. Epub 2012 Aug 23.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL 32827, USA.

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http://dx.doi.org/10.1021/bi300817dDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3490227PMC
September 2012

The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis.

Biochemistry 2011 Jan 13;50(1):144-50. Epub 2010 Dec 13.

Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, United States.

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http://dx.doi.org/10.1021/bi101819mDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3061978PMC
January 2011

Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.

Biochemistry 2010 Jul;49(27):5810-6

Department of Biochemistry, The University of Mississippi Medical Center, Jackson, Mississippi 39216-4505, USA.

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http://dx.doi.org/10.1021/bi1004969DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2913433PMC
July 2010

Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.

Biochemistry 2010 Jul;49(27):5810-6

Department of Biochemistry, The University of Mississippi Medical Center, Jackson, Mississippi 39216-4505, USA.

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http://dx.doi.org/10.1021/bi1004969DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2913433PMC
July 2010

Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis.

Biochemistry 2009 Mar;48(11):2442-7

Department of Biochemistry, The University of Mississippi Medical Center, Jackson, Mississippi 39216-4505, USA.

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http://dx.doi.org/10.1021/bi802166cDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2765563PMC
March 2009