Coenzyme B12 Enzymes Part B: Volume 669

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Informationen zum Autor I am currently Professor of Chemistry and Biological Chemistry at the University of Michigan in Ann Arbor. My research interests center on enzyme mechanisms and protein structure and design. We are currently working on a variety of research projects. In particular, we have a long-standing interest in enzymes that use free radicals to catalyze a variety of unusual chemical transformations. More recently, we have become interested in enzymes involved in hydrocarbon biosynthesis, many of which have novel mechanisms and are of practical interest for the biosynthesis of next-generation biofuels. We are also interested in understanding in molecular detail how enzymes interact with abiological surfaces as this is key to many industrial and biomedical applications where enzymes are immobilized on solid supports. More information about my research can be found here:http://www.lsa.umich.edu/chem/people/faculty/ci.marsheneilg_ci.detail

Autorentext
I am currently Professor of Chemistry and Biological Chemistry at the University of Michigan in Ann Arbor. My research interests center on enzyme mechanisms and protein structure and design. We are currently working on a variety of research projects. In particular, we have a long-standing interest in enzymes that use free radicals to catalyze a variety of unusual chemical transformations. More recently, we have become interested in enzymes involved in hydrocarbon biosynthesis, many of which have novel mechanisms and are of practical interest for the biosynthesis of next-generation biofuels. We are also interested in understanding in molecular detail how enzymes interact with abiological surfaces as this is key to many industrial and biomedical applications where enzymes are immobilized on solid supports. More information about my research can be found here:http://www.lsa.umich.edu/chem/people/faculty/ci.marsheneilg_ci.detail

Inhalt

B12-dependent radical SAM enzymes
1. Structural characterization of cobalamin-dependent radical SAM methylases
Squire Booker Penn State University
2. Purification and characterization of sequential cobalamin-dependent radical SAM methylases ThnK and TokK in -lactam antibiotic biosynthesis
Craig Townsend Johns Hopkins University

  1. Characterization of the cobalamin-dependent radical S-adenosyl-L-methionine enzyme C-methyltransferase Fom3 in fosfomycin biosynthesis
    Tadashi Eguchi Tokyo Institute of Technology
    4. Studies of OxsB and GenK, two B12-dependent radical SAM enzymes involved in natural product biosynthesis
    Hung-Wen Liu University of Texas, Austin
    5. Purification and structural elucidation of the cobalamin-dependent radical SAM enzyme OxsB
    Jennifer Bridwell-Rabb University of Michigan

    Methods for studying the mechanisms of B12 enzymes
    6. Computational investigations of B12-dependent enzymatic reactions
    Pawel Kozlowski University of Louisville, Kentucky
    7. Using kinetic isotope effects to probe the mechanisms of adenosylcobalamin-dependent enzymes
    Neil Marsh University of Michigan
    8. Steady-state and pre-steady state kinetic analysis of ornithine 4,5-aminomutase
    Kirsten Wolthers University of British Columbia
    9. Structural characterization of radical intermediates in reaction of lysine 5,6-aminomutase by EPR, ENDOR, and ESEEM
    Shyue-Chu Ke National Dong Hwa University, Taiwan
    10. Solvent-protein-reaction dynamical coupling in B12 enzyme catalysis
    Kurt Warncke Emory University, Atlanta
    11. Investigating radical pair reaction dynamics of B12 coenzymes using magnetic field effects
    Alex Jones National Physical Laboratory, U.K.
    12. Investigating radical pair reaction dynamics of B12 coenzymes using time-resolved electron paramagnetic resonance spectroscopy
    Alex Jones National Physical Laboratory, U.K.
    13. Time-resolved spectroscopy: Advances in understanding the electronic structure and dynamics of cobalamins
    Roseanne Sension and James enner-Hahn University of Michigan
    14. MCD and Raman Spectroscopy of cobalamin-dependent enzymes
    Thomas Brunold University of Wisconsin, Madison

Weitere Informationen

  • Allgemeine Informationen
    • GTIN 09780323955577
    • Genre Biology
    • Editor Neil Marsh
    • Sprache Englisch
    • Anzahl Seiten 384
    • Herausgeber Elsevier Science & Technology
    • Größe H229mm x B152mm
    • Jahr 2022
    • EAN 9780323955577
    • Format Fester Einband
    • ISBN 978-0-323-95557-7
    • Veröffentlichung 01.06.2022
    • Titel Coenzyme B12 Enzymes Part B: Volume 669
    • Gewicht 750g

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