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Article ; Online: Insights into the Biochemistry, Evolution, and Biotechnological Applications of the Ten-Eleven Translocation (TET) Enzymes.

Parker, Mackenzie J / Weigele, Peter R / Saleh, Lana

2019 Volume 58, Issue 6, Page(s) 450–467

Abstract: A tight link exists between patterns of DNA methylation at carbon 5 of cytosine and differential gene expression in mammalian tissues. Indeed, aberrant DNA methylation results in various human diseases, including neurologic and immune disorders, and ... ...

Abstract	A tight link exists between patterns of DNA methylation at carbon 5 of cytosine and differential gene expression in mammalian tissues. Indeed, aberrant DNA methylation results in various human diseases, including neurologic and immune disorders, and contributes to the initiation and progression of various cancers. Proper DNA methylation depends on the fidelity and control of the underlying mechanisms that write, maintain, and erase these epigenetic marks. In this Perspective, we address one of the key players in active demethylation: the ten-eleven translocation enzymes or TETs. These enzymes belong to the Fe
MeSH term(s)	5-Methylcytosine/metabolism ; Amino Acid Sequence ; Animals ; Biological Evolution ; DNA/chemistry ; DNA/metabolism ; DNA Methylation ; Dioxygenases/chemistry ; Dioxygenases/genetics ; Dioxygenases/metabolism ; Epigenesis, Genetic ; Gene Expression Regulation ; Humans ; Protein Conformation ; Sequence Homology ; Substrate Specificity
Chemical Substances	5-Methylcytosine (6R795CQT4H) ; DNA (9007-49-2) ; Dioxygenases (EC 1.13.11.-)
Language	English
Publishing date	2019-01-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.8b01185
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Article ; Online: Identification of 2-Sulfonyl/Sulfonamide Pyrimidines as Covalent Inhibitors of WRN Using a Multiplexed High-Throughput Screening Assay.

Parker, Mackenzie J / Lee, Hyelee / Yao, Shihua / Irwin, Sean / Hwang, Sunil / Belanger, Kylie / de Mare, Sofia Woo / Surgenor, Richard / Yan, Lu / Gee, Patricia / Morla, Shravan / Puyang, Xiaoling / Hsiao, Peng / Zeng, Hao / Zhu, Ping / Korpal, Manav / Dransfield, Paul / Bolduc, David M / Larsen, Nicholas A

Biochemistry

2023 Volume 62, Issue 14, Page(s) 2147–2160

Abstract: Werner syndrome protein (WRN) is a multifunctional enzyme with helicase, ATPase, and exonuclease activities that are necessary for numerous DNA-related transactions in the human cell. Recent studies identified WRN as a synthetic lethal target in cancers ... ...

Abstract	Werner syndrome protein (WRN) is a multifunctional enzyme with helicase, ATPase, and exonuclease activities that are necessary for numerous DNA-related transactions in the human cell. Recent studies identified WRN as a synthetic lethal target in cancers characterized by genomic microsatellite instability resulting from defects in DNA mismatch repair pathways. WRN's helicase activity is essential for the viability of these high microsatellite instability (MSI-H) cancers and thus presents a therapeutic opportunity. To this end, we developed a multiplexed high-throughput screening assay that monitors exonuclease, ATPase, and helicase activities of full-length WRN. This screening campaign led to the discovery of 2-sulfonyl/sulfonamide pyrimidine derivatives as novel covalent inhibitors of WRN helicase activity. The compounds are specific for WRN versus other human RecQ family members and show competitive behavior with ATP. Examination of these novel chemical probes established the sulfonamide NH group as a key driver of compound potency. One of the leading compounds, H3B-960, showed consistent activities in a range of assays (IC
MeSH term(s)	Humans ; Werner Syndrome ; Exodeoxyribonucleases/genetics ; RecQ Helicases/genetics ; RecQ Helicases/metabolism ; High-Throughput Screening Assays ; Microsatellite Instability ; Werner Syndrome Helicase/metabolism ; Neoplasms
Chemical Substances	Exodeoxyribonucleases (EC 3.1.-) ; RecQ Helicases (EC 3.6.4.12) ; Werner Syndrome Helicase (EC 3.6.4.12) ; WRN protein, human (EC 3.6.4.12)
Language	English
Publishing date	2023-07-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.2c00599
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Article ; Online: Choosing the right metal: case studies of class I ribonucleotide reductases.

Huang, Mingxia / Parker, Mackenzie J / Stubbe, JoAnne

The Journal of biological chemistry

2014 Volume 289, Issue 41, Page(s) 28104–28111

Abstract: Over one-third of all proteins require metallation for function (Waldron, K. J., Rutherford, J. C., Ford, D., and Robinson, N.J. (2009) Nature 460, 823-830). As biochemical studies of most proteins depend on their isolation subsequent to recombinant ... ...

Abstract	Over one-third of all proteins require metallation for function (Waldron, K. J., Rutherford, J. C., Ford, D., and Robinson, N.J. (2009) Nature 460, 823-830). As biochemical studies of most proteins depend on their isolation subsequent to recombinant expression (i.e. they are seldom purified from their host organism), there is no gold standard to assess faithful metallocofactor assembly and associated function. The biosynthetic machinery for metallocofactor formation in the recombinant expression system may be absent, inadequately expressed, or incompatible with a heterologously expressed protein. A combination of biochemical and genetic studies has led to the identification of key proteins involved in biosynthesis and likely repair of the metallocofactor of ribonucleotide reductases in both bacteria and the budding yeast. In this minireview, we will discuss the recent progress in understanding controlled delivery of metal, oxidants, and reducing equivalents for cofactor assembly in ribonucleotide reductases and highlight issues associated with controlling Fe/Mn metallation and avoidance of mismetallation.
MeSH term(s)	Cations, Divalent ; Escherichia coli/chemistry ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Expression ; Iron/chemistry ; Iron/metabolism ; Manganese/chemistry ; Manganese/metabolism ; Models, Molecular ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Ribonucleotide Reductases/chemistry ; Ribonucleotide Reductases/genetics ; Ribonucleotide Reductases/metabolism ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Species Specificity ; Structure-Activity Relationship
Chemical Substances	Cations, Divalent ; Escherichia coli Proteins ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Manganese (42Z2K6ZL8P) ; Iron (E1UOL152H7) ; Ribonucleotide Reductases (EC 1.17.4.-)
Language	English
Publishing date	2014-08-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.R114.596684
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Article ; Online: Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.

Parker, Mackenzie J / Zhu, Xuling / Stubbe, JoAnne

Biochemistry

2014 Volume 53, Issue 4, Page(s) 766–776

Abstract: The class Ib ribonucleotide reductase (RNR) isolated from Bacillus subtilis was recently purified as a 1:1 ratio of NrdE (α) and NrdF (β) subunits and determined to have a dimanganic-tyrosyl radical (Mn(III)2-Y·) cofactor. The activity of this RNR and ... ...

Abstract	The class Ib ribonucleotide reductase (RNR) isolated from Bacillus subtilis was recently purified as a 1:1 ratio of NrdE (α) and NrdF (β) subunits and determined to have a dimanganic-tyrosyl radical (Mn(III)2-Y·) cofactor. The activity of this RNR and the one reconstituted from recombinantly expressed NrdE and reconstituted Mn(III)2-Y· NrdF using dithiothreitol as the reductant, however, was low (160 nmol min(-1) mg(-1)). The apparent tight affinity between the two subunits, distinct from all class Ia RNRs, suggested that B. subtilis RNR might be the protein that yields to the elusive X-ray crystallographic characterization of an "active" RNR complex. We now report our efforts to optimize the activity of B. subtilis RNR by (1) isolation of NrdF with a homogeneous cofactor, and (2) identification and purification of the endogenous reductant(s). Goal one was achieved using anion exchange chromatography to separate apo-/mismetalated-NrdFs from Mn(III)2-Y· NrdF, yielding enzyme containing 4 Mn and 1 Y·/β2. Goal two was achieved by cloning, expressing, and purifying TrxA (thioredoxin), YosR (a glutaredoxin-like thioredoxin), and TrxB (thioredoxin reductase). The success of both goals increased the specific activity to ~1250 nmol min(-1) mg(-1) using a 1:1 mixture of NrdE:Mn(III)2-Y· NrdF and either TrxA or YosR and TrxB. The quaternary structures of NrdE, NrdF, and NrdE:NrdF (1:1) were characterized by size exclusion chromatography and analytical ultracentrifugation. At physiological concentrations (~1 μM), NrdE is a monomer (α) and Mn(III)2-Y· NrdF is a dimer (β2). A 1:1 mixture of NrdE:NrdF, however, is composed of a complex mixture of structures in contrast to expectations.
MeSH term(s)	Bacillus subtilis/enzymology ; Bacterial Proteins/chemistry ; Biocatalysis ; Glutaredoxins/chemistry ; Glutaredoxins/genetics ; Glutaredoxins/isolation & purification ; Manganese/chemistry ; Oxidation-Reduction ; Protein Structure, Quaternary ; Protein Subunits/chemistry ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Ribonucleotide Reductases/chemistry ; Thioredoxin-Disulfide Reductase/chemistry ; Thioredoxin-Disulfide Reductase/genetics ; Thioredoxin-Disulfide Reductase/isolation & purification ; Thioredoxins/chemistry ; Thioredoxins/genetics ; Thioredoxins/isolation & purification
Chemical Substances	Bacterial Proteins ; Glutaredoxins ; Protein Subunits ; Recombinant Proteins ; Manganese (42Z2K6ZL8P) ; Thioredoxins (52500-60-4) ; Ribonucleotide Reductases (EC 1.17.4.-) ; Thioredoxin-Disulfide Reductase (EC 1.8.1.9)
Language	English
Publishing date	2014-01-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi401056e
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Article: Bacillus subtilis Class Ib Ribonucleotide Reductase: High Activity and Dynamic Subunit Interactions

Parker, Mackenzie J / Zhu Xuling / Stubbe JoAnne

Biochemistry. 2014 Feb. 04, v. 53, no. 4

2014

Abstract: The class Ib ribonucleotide reductase (RNR) isolated from Bacillus subtilis was recently purified as a 1:1 ratio of NrdE (Î±) and NrdF (Î²) subunits and determined to have a dimanganic-tyrosyl radical (Mná´µá´µá´µâ-YÂ·) cofactor. The activity of this ... ...

Abstract	The class Ib ribonucleotide reductase (RNR) isolated from Bacillus subtilis was recently purified as a 1:1 ratio of NrdE (Î±) and NrdF (Î²) subunits and determined to have a dimanganic-tyrosyl radical (Mná´µá´µá´µâ-YÂ·) cofactor. The activity of this RNR and the one reconstituted from recombinantly expressed NrdE and reconstituted Mná´µá´µá´µâ-YÂ· NrdF using dithiothreitol as the reductant, however, was low (160 nmol minâÂ¹ mgâÂ¹). The apparent tight affinity between the two subunits, distinct from all class Ia RNRs, suggested that B. subtilis RNR might be the protein that yields to the elusive X-ray crystallographic characterization of an âactiveâ RNR complex. We now report our efforts to optimize the activity of B. subtilis RNR by (1) isolation of NrdF with a homogeneous cofactor, and (2) identification and purification of the endogenous reductant(s). Goal one was achieved using anion exchange chromatography to separate apo-/mismetalated-NrdFs from Mná´µá´µá´µâ-YÂ· NrdF, yielding enzyme containing 4 Mn and 1 YÂ·/Î²â. Goal two was achieved by cloning, expressing, and purifying TrxA (thioredoxin), YosR (a glutaredoxin-like thioredoxin), and TrxB (thioredoxin reductase). The success of both goals increased the specific activity to â¼1250 nmol minâÂ¹ mgâÂ¹ using a 1:1 mixture of NrdE:Mná´µá´µá´µâ-YÂ· NrdF and either TrxA or YosR and TrxB. The quaternary structures of NrdE, NrdF, and NrdE:NrdF (1:1) were characterized by size exclusion chromatography and analytical ultracentrifugation. At physiological concentrations (â¼1 Î¼M), NrdE is a monomer (Î±) and Mná´µá´µá´µâ-YÂ· NrdF is a dimer (Î²â). A 1:1 mixture of NrdE:NrdF, however, is composed of a complex mixture of structures in contrast to expectations.
Keywords	Bacillus subtilis ; X-ray diffraction ; anion exchange chromatography ; dithiothreitol ; gel chromatography ; manganese ; reducing agents ; ribonucleotide reductase ; ultracentrifugation
Language	English
Dates of publication	2014-0204
Size	p. 766-776.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021%2Fbi401056e
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Article: Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation

Soule, Jess / Gnann, Andrew D / Gonzalez, Reyaz / Parker, Mackenzie J / McKenna, Kylie C / Nguyen, Son V / Phan, Ngan T / Wicht, Denyce K / Dowling, Daniel P

Biochemical and biophysical research communications. 2020 Jan. 29, v. 522, no. 1

2020

Abstract: Methyl sulfur compounds are a rich source of environmental sulfur for microorganisms, but their use requires redox systems. The bacterial sfn and msu operons contain two-component flavin-dependent monooxygenases for dimethylsulfone (DMSO₂) assimilation: ... ...

Abstract	Methyl sulfur compounds are a rich source of environmental sulfur for microorganisms, but their use requires redox systems. The bacterial sfn and msu operons contain two-component flavin-dependent monooxygenases for dimethylsulfone (DMSO₂) assimilation: SfnG converts DMSO₂ to methanesulfinate (MSI–), and MsuD converts methanesulfonate (MS–) to sulfite. However, the enzymatic oxidation of MSI– to MS– has not been demonstrated, and the function of the last enzyme of the msu operon (MsuC) is unresolved. We employed crystallographic and biochemical studies to identify the function of MsuC from Pseudomonas fluorescens. The crystal structure of MsuC adopts the acyl-CoA dehydrogenase fold with putative binding sites for flavin and MSI–, and functional assays of MsuC in the presence of its oxidoreductase MsuE, FMN, and NADH confirm the enzymatic generation of MS–. These studies reveal that MsuC converts MSI– to MS– in sulfite biosynthesis from DMSO₂.
Keywords	Pseudomonas fluorescens ; acyl-CoA dehydrogenase ; biosynthesis ; crystal structure ; operon ; oxidation ; research ; sulfites ; sulfur ; unspecific monooxygenase
Language	English
Dates of publication	2020-0129
Size	p. 107-112.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2019.11.008
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Article ; Online: An endogenous dAMP ligand in

Parker, Mackenzie J / Maggiolo, Ailiena O / Thomas, William C / Kim, Albert / Meisburger, Steve P / Ando, Nozomi / Boal, Amie K / Stubbe, JoAnne

Proceedings of the National Academy of Sciences of the United States of America

2018 Volume 115, Issue 20, Page(s) E4594–E4603

Abstract: The high fidelity of DNA replication and repair is attributable, in part, to the allosteric regulation of ribonucleotide reductases (RNRs) that maintains proper deoxynucleotide pool sizes and ratios in vivo. In class Ia RNRs, ATP (stimulatory) and dATP ( ... ...

Abstract	The high fidelity of DNA replication and repair is attributable, in part, to the allosteric regulation of ribonucleotide reductases (RNRs) that maintains proper deoxynucleotide pool sizes and ratios in vivo. In class Ia RNRs, ATP (stimulatory) and dATP (inhibitory) regulate activity by binding to the ATP-cone domain at the N terminus of the large α subunit and altering the enzyme's quaternary structure. Class Ib RNRs, in contrast, have a partial cone domain and have generally been found to be insensitive to dATP inhibition. An exception is the
MeSH term(s)	Allosteric Regulation ; Bacillus subtilis/enzymology ; Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Deoxyadenine Nucleotides/chemistry ; Deoxyadenine Nucleotides/metabolism ; Ligands ; Protein Binding ; Protein Conformation ; Ribonucleotide Reductases/chemistry ; Ribonucleotide Reductases/genetics ; Ribonucleotide Reductases/metabolism ; Scattering, Small Angle ; Substrate Specificity
Chemical Substances	Bacterial Proteins ; Deoxyadenine Nucleotides ; Ligands ; 2'-deoxy-5'-adenosine monophosphate (653-63-4) ; Ribonucleotide Reductases (EC 1.17.4.-) ; 2'-deoxyadenosine triphosphate (K8KCC8SH6N)
Language	English
Publishing date	2018-04-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1800356115
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Article ; Online: Phage-encoded ten-eleven translocation dioxygenase (TET) is active in C5-cytosine hypermodification in DNA.

Burke, Evan J / Rodda, Samuel S / Lund, Sean R / Sun, Zhiyi / Zeroka, Malcolm R / O'Toole, Katherine H / Parker, Mackenzie J / Doshi, Dharit S / Guan, Chudi / Lee, Yan-Jiun / Dai, Nan / Hough, David M / Shnider, Daria A / Corrêa, Ivan R / Weigele, Peter R / Saleh, Lana

Proceedings of the National Academy of Sciences of the United States of America

2021 Volume 118, Issue 26

Abstract: TET/JBP (ten-eleven translocation/base J binding protein) enzymes are iron(II)- and 2-oxo-glutarate-dependent dioxygenases that are found in all kingdoms of life and oxidize 5-methylpyrimidines on the polynucleotide level. Despite their prevalence, few ... ...

Abstract	TET/JBP (ten-eleven translocation/base J binding protein) enzymes are iron(II)- and 2-oxo-glutarate-dependent dioxygenases that are found in all kingdoms of life and oxidize 5-methylpyrimidines on the polynucleotide level. Despite their prevalence, few examples have been biochemically characterized. Among those studied are the metazoan TET enzymes that oxidize 5-methylcytosine in DNA to hydroxy, formyl, and carboxy forms and the euglenozoa JBP dioxygenases that oxidize thymine in the first step of base J biosynthesis. Both enzymes have roles in epigenetic regulation. It has been hypothesized that all TET/JBPs have their ancestral origins in bacteriophages, but only eukaryotic orthologs have been described. Here we demonstrate the 5mC-dioxygenase activity of several phage TETs encoded within viral metagenomes. The clustering of these TETs in a phylogenetic tree correlates with the sequence specificity of their genomically cooccurring cytosine C5-methyltransferases, which install the methyl groups upon which TETs operate. The phage TETs favor Gp5mC dinucleotides over the 5mCpG sites targeted by the eukaryotic TETs and are found within gene clusters specifying complex cytosine modifications that may be important for DNA packaging and evasion of host restriction.
MeSH term(s)	5-Methylcytosine/metabolism ; Amino Acid Sequence ; Bacteriophages/metabolism ; DNA/metabolism ; DNA Methylation ; Dioxygenases ; Hydroxylation ; Metagenomics ; Nucleotide Motifs/genetics ; Oxidation-Reduction ; Phylogeny
Chemical Substances	5-Methylcytosine (6R795CQT4H) ; DNA (9007-49-2) ; Dioxygenases (EC 1.13.11.-)
Language	English
Publishing date	2021-06-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2026742118
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Article ; Online: Glutamate 52-β at the α/β subunit interface of

Lin, Qinghui / Parker, Mackenzie J / Taguchi, Alexander T / Ravichandran, Kanchana / Kim, Albert / Kang, Gyunghoon / Shao, Jimin / Drennan, Catherine L / Stubbe, JoAnne

The Journal of biological chemistry

2017 Volume 292, Issue 22, Page(s) 9229–9239

Abstract: Ribonucleotide reductases (RNRs) catalyze the conversion of nucleoside diphosphate substrates (S) to deoxynucleotides with allosteric effectors (e) controlling their relative ratios and amounts, crucial for fidelity of DNA replication and repair. ...

Abstract	Ribonucleotide reductases (RNRs) catalyze the conversion of nucleoside diphosphate substrates (S) to deoxynucleotides with allosteric effectors (e) controlling their relative ratios and amounts, crucial for fidelity of DNA replication and repair.
MeSH term(s)	Amino Acid Substitution ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Molecular Docking Simulation ; Mutation, Missense ; Ribonucleotide Reductases/chemistry ; Ribonucleotide Reductases/metabolism
Chemical Substances	Escherichia coli Proteins ; NrdB protein, E coli (EC 1.17.4.-) ; Ribonucleotide Reductases (EC 1.17.4.-)
Language	English
Publishing date	2017-04-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M117.783092
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Article ; Online: Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation.

Soule, Jess / Gnann, Andrew D / Gonzalez, Reyaz / Parker, Mackenzie J / McKenna, Kylie C / Nguyen, Son V / Phan, Ngan T / Wicht, Denyce K / Dowling, Daniel P

Biochemical and biophysical research communications

2019 Volume 522, Issue 1, Page(s) 107–112

Abstract	Methyl sulfur compounds are a rich source of environmental sulfur for microorganisms, but their use requires redox systems. The bacterial sfn and msu operons contain two-component flavin-dependent monooxygenases for dimethylsulfone (DMSO
MeSH term(s)	Acyl-CoA Dehydrogenase/metabolism ; Bacterial Proteins/metabolism ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; Dimethyl Sulfoxide/chemistry ; Flavins/chemistry ; Magnetic Resonance Spectroscopy ; Mesylates/chemistry ; Molecular Docking Simulation ; Oxidoreductases/metabolism ; Oxygen/chemistry ; Protein Structure, Secondary ; Pseudomonas fluorescens/enzymology ; Structure-Activity Relationship ; Sulfides/chemistry ; Sulfones/chemistry ; Sulfur/chemistry ; Thiophenes/chemistry
Chemical Substances	Bacterial Proteins ; Flavins ; Mesylates ; Sulfides ; Sulfones ; Thiophenes ; methanesulfonic acid (12EH9M7279) ; Sulfur (70FD1KFU70) ; Oxidoreductases (EC 1.-) ; Acyl-CoA Dehydrogenase (EC 1.3.8.7) ; Oxygen (S88TT14065) ; Dimethyl Sulfoxide (YOW8V9698H) ; dibenzothiophene (Z3D4AJ1R48)
Language	English
Publishing date	2019-11-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2019.11.008
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