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  1. Article ; Online: Not a "they" but a "we": The microbiome helps promote our well-being.

    Ragsdale, Stephen W

    The Journal of biological chemistry

    2021  Volume 298, Issue 2, Page(s) 101511

    Abstract: Anaerobic microbes in the human gut produce beneficial and harmful compounds, as well as neutral compounds like trimethylamine, which undergoes microbial metabolism or host-catalyzed transformation into proatherogenic trimethylamine-N-oxide. Ellenbogen ... ...

    Abstract Anaerobic microbes in the human gut produce beneficial and harmful compounds, as well as neutral compounds like trimethylamine, which undergoes microbial metabolism or host-catalyzed transformation into proatherogenic trimethylamine-N-oxide. Ellenbogen et al. identified a microbiome-associated demethylase that short-circuits the production of trimethylamine-N-oxide from the metabolite γ-butyrobetaine and instead produces methyltetrahydrofolate, a key intermediate in the microbial production of beneficial small-chain fatty acids. This article highlights an example of how the microbiome is integrally involved in producing metabolites that support our health and in preventing the formation of compounds that promote disease.
    MeSH term(s) Betaine/analogs & derivatives ; Carnitine ; Eubacterium ; Gastrointestinal Microbiome ; Humans ; Methylamines/metabolism ; Methyltransferases/metabolism ; Microbiota ; Oxides ; Vitamin B 12
    Chemical Substances Methylamines ; Oxides ; Betaine (3SCV180C9W) ; gamma-butyrobetaine (407-64-7) ; Methyltransferases (EC 2.1.1.-) ; Vitamin B 12 (P6YC3EG204) ; Carnitine (S7UI8SM58A)
    Language English
    Publishing date 2021-12-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Comment
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2021.101511
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  2. Article ; Online: Elusive microbe that consumes ethane found under the sea.

    Ragsdale, Stephen W

    Nature

    2019  Volume 568, Issue 7750, Page(s) 40–41

    MeSH term(s) Archaea ; Ethane ; Hydrocarbons ; Oxidation-Reduction
    Chemical Substances Hydrocarbons ; Ethane (L99N5N533T)
    Language English
    Publishing date 2019-03-27
    Publishing country England
    Document type News ; Comment
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/d41586-019-00842-2
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  3. Article ; Online: Stealth reactions driving carbon fixation.

    Ragsdale, Stephen W

    Science (New York, N.Y.)

    2018  Volume 359, Issue 6375, Page(s) 517–518

    MeSH term(s) Bacterial Physiological Phenomena ; Carbon Cycle
    Language English
    Publishing date 2018--02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.aar6329
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  4. Article ; Online: Microbiology: Deep-sea secrets of butane metabolism.

    Ragsdale, Stephen W

    Nature

    2016  Volume 539, Issue 7629, Page(s) 367–368

    MeSH term(s) Butanes/metabolism ; Oceans and Seas ; Seawater ; Water Microbiology
    Chemical Substances Butanes
    Language English
    Publishing date 2016--17
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/539367a
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  5. Article ; Online: Targeting methanogenesis with a nitrooxypropanol bullet.

    Ragsdale, Stephen W

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

    2016  Volume 113, Issue 22, Page(s) 6100–6101

    MeSH term(s) Animals ; Methane ; Rumen
    Chemical Substances Methane (OP0UW79H66)
    Language English
    Publishing date 2016-05-31
    Publishing country United States
    Document type Editorial ; Research Support, U.S. Gov't, Non-P.H.S. ; Comment
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1606107113
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  6. Article ; Online: Efficient, Light-Driven Reduction of CO

    White, David W / Esckilsen, Daniel / Lee, Seung Kyu / Ragsdale, Stephen W / Dyer, R Brian

    The journal of physical chemistry letters

    2022  Volume 13, Issue 24, Page(s) 5553–5556

    Abstract: The solar conversion of ... ...

    Abstract The solar conversion of CO
    MeSH term(s) Aldehyde Oxidoreductases ; Cadmium Compounds ; Carbon Dioxide ; Carbon Monoxide/chemistry ; Multienzyme Complexes ; Nanotubes ; Selenium Compounds
    Chemical Substances Cadmium Compounds ; Multienzyme Complexes ; Selenium Compounds ; Carbon Dioxide (142M471B3J) ; Carbon Monoxide (7U1EE4V452) ; Aldehyde Oxidoreductases (EC 1.2.-) ; carbon monoxide dehydrogenase (EC 1.2.7.4)
    Language English
    Publishing date 2022-06-13
    Publishing country United States
    Document type Journal Article
    ISSN 1948-7185
    ISSN (online) 1948-7185
    DOI 10.1021/acs.jpclett.2c01412
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  7. Article ; Online: An unlikely heme chaperone confirmed at last.

    Fleischhacker, Angela S / Ragsdale, Stephen W

    The Journal of biological chemistry

    2018  Volume 293, Issue 37, Page(s) 14569–14570

    Abstract: Labile heme, as opposed to heme that is tightly bound within proteins, is thought to require a chaperone to be trafficked within the cell due to its cytotoxicity, but the identity of this chaperone was not known. A new study reveals that an unlikely ... ...

    Abstract Labile heme, as opposed to heme that is tightly bound within proteins, is thought to require a chaperone to be trafficked within the cell due to its cytotoxicity, but the identity of this chaperone was not known. A new study reveals that an unlikely protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), is a heme chaperone that binds and transfers labile heme to downstream target proteins. These results provide a new framework for understanding heme homeostasis and raise intriguing questions regarding the intersection of heme transport, carbohydrate metabolism, and intracellular signaling.
    MeSH term(s) Animals ; Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry ; Glyceraldehyde-3-Phosphate Dehydrogenases/genetics ; Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism ; Heme/chemistry ; Heme/metabolism ; Humans ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Binding
    Chemical Substances Molecular Chaperones ; Heme (42VZT0U6YR) ; Glyceraldehyde-3-Phosphate Dehydrogenases (EC 1.2.1.-)
    Language English
    Publishing date 2018-09-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.H118.005247
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  8. Article ; Online: Regulation of protein function and degradation by heme, heme responsive motifs, and CO.

    Fleischhacker, Angela S / Sarkar, Anindita / Liu, Liu / Ragsdale, Stephen W

    Critical reviews in biochemistry and molecular biology

    2021  Volume 57, Issue 1, Page(s) 16–47

    Abstract: Heme is an essential biomolecule and cofactor involved in a myriad of biological processes. In this review, we focus on how heme binding to heme regulatory motifs (HRMs), catalytic sites, and gas signaling molecules as well as how changes in the heme ... ...

    Abstract Heme is an essential biomolecule and cofactor involved in a myriad of biological processes. In this review, we focus on how heme binding to heme regulatory motifs (HRMs), catalytic sites, and gas signaling molecules as well as how changes in the heme redox state regulate protein structure, function, and degradation. We also relate these heme-dependent changes to the affected metabolic processes. We center our discussion on two HRM-containing proteins: human heme oxygenase-2, a protein that binds and degrades heme (releasing Fe
    MeSH term(s) Heme/chemistry ; Heme/metabolism ; Humans ; Oxidation-Reduction ; Protein Binding ; Receptors, Cytoplasmic and Nuclear/metabolism ; Repressor Proteins/metabolism
    Chemical Substances Receptors, Cytoplasmic and Nuclear ; Repressor Proteins ; Heme (42VZT0U6YR)
    Language English
    Publishing date 2021-09-13
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 1000977-2
    ISSN 1549-7798 ; 1381-3455 ; 1040-9238
    ISSN (online) 1549-7798
    ISSN 1381-3455 ; 1040-9238
    DOI 10.1080/10409238.2021.1961674
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  9. Article: Biochemistry of methyl-coenzyme M reductase: the nickel metalloenzyme that catalyzes the final step in synthesis and the first step in anaerobic oxidation of the greenhouse gas methane.

    Ragsdale, Stephen W

    Metal ions in life sciences

    2014  Volume 14, Page(s) 125–145

    Abstract: Methane, the major component of natural gas, has been in use in human civilization since ancient times as a source of fuel and light. Methanogens are responsible for synthesis of most of the methane found on Earth. The enzyme responsible for catalyzing ... ...

    Abstract Methane, the major component of natural gas, has been in use in human civilization since ancient times as a source of fuel and light. Methanogens are responsible for synthesis of most of the methane found on Earth. The enzyme responsible for catalyzing the chemical step of methanogenesis is methyl-coenzyme M reductase (MCR), a nickel enzyme that contains a tetrapyrrole cofactor called coenzyme F430, which can traverse the Ni(I), (II), and (III) oxidation states. MCR and methanogens are also involved in anaerobic methane oxidation. This review describes structural, kinetic, and computational studies aimed at elucidating the mechanism of MCR. Such studies are expected to impact the many ramifications of methane in our society and environment, including energy production and greenhouse gas warming.
    MeSH term(s) Anaerobiosis ; Animals ; Catalysis ; Energy-Generating Resources ; Environment ; Greenhouse Effect ; Humans ; Metalloproteins/chemistry ; Metalloproteins/metabolism ; Methane/biosynthesis ; Methane/chemistry ; Methane/metabolism ; Models, Molecular ; Nickel/chemistry ; Nickel/metabolism ; Oxidation-Reduction ; Oxidoreductases/chemistry ; Oxidoreductases/metabolism ; Protein Structure, Tertiary
    Chemical Substances Metalloproteins ; Nickel (7OV03QG267) ; Oxidoreductases (EC 1.-) ; methyl coenzyme M reductase (EC 2.8.4.1) ; Methane (OP0UW79H66)
    Language English
    Publishing date 2014
    Publishing country Netherlands
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ISSN 1559-0836
    ISSN 1559-0836
    DOI 10.1007/978-94-017-9269-1_6
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  10. Article ; Online: 13

    James, Christopher D / Wiley, Seth / Ragsdale, Stephen W / Hoffman, Brian M

    Journal of the American Chemical Society

    2020  Volume 142, Issue 36, Page(s) 15362–15370

    Abstract: EPR and Electron Nuclear Double Resonance spectroscopies here characterize CO binding to the active-site A cluster of wild-type (WT) Acetyl-CoA Synthase (ACS) and two variants, F229W and F229A. The A-cluster binds CO to a proximal Ni ( ... ...

    Abstract EPR and Electron Nuclear Double Resonance spectroscopies here characterize CO binding to the active-site A cluster of wild-type (WT) Acetyl-CoA Synthase (ACS) and two variants, F229W and F229A. The A-cluster binds CO to a proximal Ni (Ni
    MeSH term(s) Acetyl Coenzyme A/chemistry ; Acetyl Coenzyme A/metabolism ; Binding Sites ; Carbon Isotopes ; Carbon Monoxide/chemistry ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Models, Molecular ; Molecular Conformation ; Nuclear Magnetic Resonance, Biomolecular
    Chemical Substances Carbon Isotopes ; Acetyl Coenzyme A (72-89-9) ; Carbon Monoxide (7U1EE4V452) ; Carbon-13 (FDJ0A8596D)
    Language English
    Publishing date 2020-08-26
    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 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.0c05950
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