Electrochemical cofactor recycling of bacterial microcompartments.

Autor: Sutter M; MSU-DOE Plant Research Laboratory, Michigan State University; East Lansing, MI 48824, USA.; Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA.; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA., Utschig LM; Chemical Sciences and Engineering Division, Argonne National Laboratory; Lemont, IL 60439, USA., Niklas J; Chemical Sciences and Engineering Division, Argonne National Laboratory; Lemont, IL 60439, USA., Paul S; Molecular Foundry Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA., Kahan DN; Biophysics Graduate Program, University of California; Berkeley, CA, 94720, USA., Gupta S; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA., Poluektov OG; Chemical Sciences and Engineering Division, Argonne National Laboratory; Lemont, IL 60439, USA., Ferlez BH; MSU-DOE Plant Research Laboratory, Michigan State University; East Lansing, MI 48824, USA., Tefft NM; Department of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824, USA., TerAvest MA; Department of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824, USA., Hickey DP; Department of Chemical Engineering and Materials Science, Michigan State University; East Lansing, MI 48824, USA., Vermaas JV; MSU-DOE Plant Research Laboratory, Michigan State University; East Lansing, MI 48824, USA.; Department of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824, USA., Ralston CY; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA.; Molecular Foundry Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA., Kerfeld CA; MSU-DOE Plant Research Laboratory, Michigan State University; East Lansing, MI 48824, USA.; Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA.; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory; Berkeley, CA 94720, USA.; Department of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824, USA.
Jazyk: angličtina
Zdroj: BioRxiv : the preprint server for biology [bioRxiv] 2024 Jul 15. Date of Electronic Publication: 2024 Jul 15.
DOI: 10.1101/2024.07.15.603600
Abstrakt: Bacterial microcompartments (BMCs) are prokaryotic organelles that consist of a protein shell which sequesters metabolic reactions in its interior. While most of the substrates and products are relatively small and can permeate the shell, many of the encapsulated enzymes require cofactors that must be regenerated inside. We have analyzed the occurrence of an enzyme previously assigned as a cobalamin (vitamin B 12 ) reductase and, curiously, found it in many unrelated BMC types that do not employ B 12 cofactors. We propose NAD+ regeneration as a new function of this enzyme and name it MNdh, for Metabolosome NADH dehydrogenase. Its partner shell protein BMC-T SE assists in passing the generated electrons to the outside. We support this hypothesis with bioinformatic analysis, functional assays, EPR spectroscopy, protein voltammetry and structural modeling verified with X-ray footprinting. This discovery represents a new paradigm for the BMC field, identifying a new, widely occurring route for cofactor recycling and a new function for the shell as separating redox environments.
Competing Interests: Competing interests Authors declare that they have no competing interests.
Databáze: MEDLINE
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