Electrochemical cofactor recycling of bacterial microcompartments

• 成果类型: Article
• 署名作者: Sutter, Markus; Utschig, Lisa M.; Niklas, Jens; Paul, Sathi; Kahan, Darren N.; Gupta, Sayan; Poluektov, Oleg G.; Ferlez, Bryan H.; Tefft, Nicholas M.; Teravest, Michaela A.; Hickey, David P.; Vermaas, Josh V.; Ralston, Corie Y.; Kerfeld, Cheryl A.
• 署名单位: Michigan State University; United States Department of Energy (DOE); United States Department of Energy (DOE); Lawrence Berkeley National Laboratory; United States Department of Energy (DOE); Lawrence Berkeley National Laboratory; United States Department of Energy (DOE); Argonne National Laboratory; United States Department of Energy (DOE); Lawrence Berkeley National Laboratory; University of California System; University of California Berkeley; Michigan State University; Michigan State University
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-14841
• DOI: 10.1073/pnas.2414220121/-/DCSupplemental
• 发表日期: 2024-12-03
• 关键词: carboxysome shell protein; salmonella-enterica; beta-carboxysome; mechanism; organelle; encodes; operon; ccmp; pdut

摘要

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 B12) reductase and, curiously, found it in many unrelated BMC types that do not employ B12 cofactors. We propose Nicotinamide adenine dinucleotide (NAD+) regeneration as the function of this enzyme and name it Metabolosome Nicotinamide Adenine Dinucleotide Hydrogen BMC shell protein of the single layer type for electron transfer) assists in passing the generated electrons to the outside. We support this hypothesis with bioinformatic analysis, and structural modeling verified with X- ray footprinting. This finding represents a 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.