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  • 1
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    BIOCHEMISTRY. Methane--make it or break it (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawton, Thomas J -- Rosenzweig, Amy C -- New York, N.Y. -- Science. 2016 May 20;352(6288):892-3. doi: 10.1126/science.aaf7700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL 60208, USA. thomas.j.lawton@gmail.com amyr@northwestern.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27199402" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    SCIENTIFIC COMMUNITY. Preprints for the life sciences (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Jeremy M -- Bhalla, Needhi -- Bourne, Philip E -- Chalfie, Martin -- Drubin, David G -- Fraser, James S -- Greider, Carol W -- Hendricks, Michael -- Jones, Chonnettia -- Kiley, Robert -- King, Susan -- Kirschner, Marc W -- Krumholz, Harlan M -- Lehmann, Ruth -- Leptin, Maria -- Pulverer, Bernd -- Rosenzweig, Brooke -- Spiro, John E -- Stebbins, Michael -- Strasser, Carly -- Swaminathan, Sowmya -- Turner, Paul -- Vale, Ronald D -- VijayRaghavan, K -- Wolberger, Cynthia -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2016 May 20;352(6288):899-901. doi: 10.1126/science.aaf9133.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Personalized Medicine, University of Pittsburgh School of Medicine. ; Department of Molecular, Cell and Developmental Biology, University of California, Santa Cruz. ; Office of the Director, National Institutes of Health. ; Department of Biological Sciences, Columbia University. ; Department of Molecular and Cell Biology, University of California, Berkeley. ; Department of Bioengineering and Therapeutic Sciences, University of California San Francisco. ; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine. ; Department of Biology, McGill University. ; Wellcome Trust. ; Rockefeller University Press. ; Department of Systems Biology, Harvard Medical School. ; Yale School of Medicine, Yale University. ; Kimmel Center for Biology and Medicine of the Skirball Institute, Department of Cell Biology, New York University School of Medicine. ; European Molecular Biology Organization. ; The Leona M. and Harry B. Helmsley Charitable Trust. ; Simons Foundation. ; Laura and John Arnold Foundation. ; Gordon and Betty Moore Foundation. ; Nature Research Group. ; Department of Ecology and Evolutionary Biology, Yale University. ; Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California San Francisco. ron.vale@ucsf.edu. ; Department of Biotechnology, Ministry of Science and Technology, Government of India. ; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27199406" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    The biosynthesis of methanobactin (2018)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2018-03-23
    Description: Metal homeostasis poses a major challenge to microbes, which must acquire scarce elements for core metabolic processes. Methanobactin, an extensively modified copper-chelating peptide, was one of the earliest natural products shown to enable microbial acquisition of a metal other than iron. We describe the core biosynthetic machinery responsible for the characteristic posttranslational modifications that grant methanobactin its specificity and affinity for copper. A heterodimer comprising MbnB, a DUF692 family iron enzyme, and MbnC, a protein from a previously unknown family, performs a dioxygen-dependent four-electron oxidation of the precursor peptide (MbnA) to install an oxazolone and an adjacent thioamide, the characteristic methanobactin bidentate copper ligands. MbnB and MbnC homologs are encoded together and separately in many bacterial genomes, suggesting functions beyond their roles in methanobactin biosynthesis.
    Keywords: Biochemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Particulate methane monooxygenase contains only mononuclear copper centers (2019)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2019
    Description: 〈p〉Bacteria that oxidize methane to methanol are central to mitigating emissions of methane, a potent greenhouse gas. The nature of the copper active site in the primary metabolic enzyme of these bacteria, particulate methane monooxygenase (pMMO), has been controversial owing to seemingly contradictory biochemical, spectroscopic, and crystallographic results. We present biochemical and electron paramagnetic resonance spectroscopic characterization most consistent with two monocopper sites within pMMO: one in the soluble PmoB subunit at the previously assigned active site (Cu〈sub〉B〈/sub〉) and one ~2 nanometers away in the membrane-bound PmoC subunit (Cu〈sub〉C〈/sub〉). On the basis of these results, we propose that a monocopper site is able to catalyze methane oxidation in pMMO.〈/p〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    A biochemical sulfur delivery service (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2017-10-20
    Keywords: Biochemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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