Lasseur C, Verstraete W, Gros JB, Dubertret G, Rogalla F. MELISSA: a potential experiment for a precursor mission to the moon. Adv Sp Res. 1996;18:111-7. https://doi.org/10.1016/0273-1177(96)00097-X.
Lasseur C, Brunet J, De Weever H, Dixon M, Dussap G, Godia F, et al. Melissa: the European project of closed life support system. Gravitational Sp Biol. 2010;23:3-12.
Jiang J, Zhang Y, Li K, Wang Q, Gong C, Li M. Volatile fatty acids production from food waste: effects of pH, temperature, and organic loading rate. Bioresour Technol. 2013;143:525-30. https://doi.org/10.1016/j.biortech.2013.06.025.
Janssen PH, Schink B. Pathway of butyrate catabolism by Desulfobacterium cetonicum. J Bacteriol. 1995;177:3870-2. https://doi.org/10.1128/JB.177.13.3870-3872.1995.
Kornberg HL, Krebs HA. Synthesis of cell constituents from C2-units by a modified Tricarboxylic acid cycle. Nature. 1957;179:988-91. https://doi.org/10.1038/179988a0.
Erb TJ, Berg IA, Brecht V, Muller M, Fuchs G, Alber BE. Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway. Proc Natl Acad Sci. 2007;104:10631-6.
Peyraud R, Kiefer P, Christen P, Massou S, Portais J-C, Vorholt JA. Demonstration of the ethylmalonyl-CoA pathway by using 13C metabolomics. Proc Natl Acad Sci. 2009;106:4846-51.
Schneider K, Peyraud R, Kiefer P, Christen P, Delmotte N, Massou S, et al. The Ethylmalonyl-CoA pathway is used in place of the Glyoxylate cycle by Methylobacterium extorquens AM1 during growth on acetate. J Biol Chem. 2012;287:757-66.
Smejkalová H, Erb TJ, Fuchs G. Methanol assimilation in Methylobacterium extorquens AM1: demonstration of all enzymes and their regulation. PLoS One. 2010;5:e13001. https://doi.org/10.1371/journal.pone.0013001.
Leroy B, De Meur Q, Moulin C, Wegria G, Wattiez R. New insight into the photoheterotrophic growth of the isocytrate lyase-lacking purple bacterium Rhodospirillum rubrum on acetate. Microbiology. 2015;161(Pt 5):1061-72. https://doi.org/10.1099/mic.0.000067.
Bayon-Vicente G, Wattiez R, Leroy B. Global proteomic analysis reveals high light intensity adaptation strategies and polyhydroxyalkanoate production in Rhodospirillum rubrum cultivated with acetate as carbon source. Front Microbiol. 2020. https://doi.org/10.3389/fmicb.2020.00464.
Wetmore KM, Price MN, Waters RJ, Lamson JS, He J, Hoover CA, et al. Rapid Quantification of Mutant Fitness in Diverse Bacteria by Sequencing Randomly Bar-Coded Transposons. MBio. 2015;6:e00306-15.
De Meur Q, Deutschbauer A, Koch M, Wattiez R, Leroy B. Genetic plasticity and Ethylmalonyl coenzyme a pathway during acetate assimilation in Rhodospirillum rubrum S1H under photoheterotrophic conditions. Appl Environ Microbiol. 2018;84. https://doi.org/10.1128/AEM.02038-17.
Ormerod JG. The use of radioactive carbon dioxide in the measurement of carbon dioxide fixation in Rhodospirillum rubrum. Biochem J. 1956;64:373-80. https://doi.org/10.1042/bj0640373.
Hillmer P, Gest H. H2 metabolism in the photosynthetic bacterium Rhodopseudomonas capsulata: H2 production by growing cultures. J Bacteriol. 1977;129:724-31. https://doi.org/10.1128/JB.129.2.724-731.1977.
Richardson DJ, King GF, Kelly DJ, McEwan AG, Ferguson SJ, Jackson JB. The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatus on propionate or butyrate. Arch Microbiol. 1988;150:131-7. https://doi.org/10.1007/BF00425152.
McKinlay JB, Harwood CS. Carbon dioxide fixation as a central redox cofactor recycling mechanism in bacteria. Proc Natl Acad Sci. 2010;107:11669-75.
Finn RD, Attwood TK, Babbitt PC, Bateman A, Bork P, Bridge AJ, et al. InterPro in 2017-beyond protein family and domain annotations. Nucleic Acids Res. 2017;45:D190-9. https://doi.org/10.1093/nar/gkw1107.
Boynton ZL, Bennet GN, Rudolph FB. Cloning, sequencing, and expression of clustered genes encoding beta-hydroxybutyryl-coenzyme a (CoA) dehydrogenase, crotonase, and butyryl-CoA dehydrogenase from Clostridium acetobutylicum ATCC 824. J Bacteriol. 1996;178:3015-24. https://doi.org/10.1128/JB.178.11.3015-3024.1996.
Williamson G, Engel PC. Butyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction. Biochem J. 1984;218:521-9. https://doi.org/10.1042/bj2180521.
Verlinden RAJ, Hill DJ, Kenward MA, Williams CD, Radecka I. Bacterial synthesis of biodegradable polyhydroxyalkanoates. J Appl Microbiol. 2007;102:1437-49. https://doi.org/10.1111/j.1365-2672.2007.03335.x.
Moskowitz GJ, Merrick JM. Metabolism of poly-beta-hydroxybutyrate. II. Enzymatic synthesis of D-(-)-beta hydroxybutyryl coenzyme a by an enoyl hydrase from Rhodospirillum rubrum. Biochemistry. 1969;8:2748-55.
Handrick R, Reinhardt S, Schultheiss D, Reichart T, Schuler D, Jendrossek V, et al. Unraveling the function of the Rhodospirillum rubrum activator of Polyhydroxybutyrate (PHB) degradation: the activator is a PHB-granule-bound protein (Phasin). J Bacteriol. 2004;186:2466-75. https://doi.org/10.1128/JB.186.8.2466-2475.2004.
Handrick R, Technow U, Reichart T, Reinhardt S, Sander T, Jendrossek D. The activator of the Rhodospirillum rubrum PHB depolymerase is a polypeptide that is extremely resistant to high temperature (121 degrees C) and other physical or chemical stresses. FEMS Microbiol Lett. 2004;230:265-74. https://doi.org/10.1016/S0378-1097(03)00919-4.
Handrick R, Reinhardt S, Kimmig P, Jendrossek D. The "intracellular" poly (3-hydroxybutyrate) (PHB) depolymerase of Rhodospirillum rubrum is a periplasm-located protein with specificity for native PHB and with structural similarity to extracellular PHB depolymerases. J Bacteriol. 2004;186:7243-53. https://doi.org/10.1128/JB.186.21.7243-7253.2004.
Doi Y, Segawa A, Kawaguchi Y, Kunioka M. Cyclic nature of poly (3-hydroxyalkanoate) metabolism in Alcaligenes eutrophus. FEMS Microbiol Lett. 1990;55:165-9.
Taidi B, Mansfield DA, Anderson AJ. Turnover of poly (3-hydroxybutyrate) (PHB) and its influence on the molecular mass of the polymer accumulated by during batch culture. FEMS Microbiol Lett. 1995;129:201-5.
Lawrence AG, Schoenheit J, He A, Tian J, Liu P, Stubbe J, et al. Transcriptional analysis of Ralstonia eutropha genes related to poly-(R)-3-hydroxybutyrate homeostasis during batch fermentation. Appl Microbiol Biotechnol. 2005;68:663-72. https://doi.org/10.1007/s00253-005-1969-3.
Narancic T, Scollica E, Kenny ST, Gibbons H, Carr E, Brennan L, et al. Understanding the physiological roles of polyhydroxybutyrate (PHB) in Rhodospirillum rubrum S1 under aerobic chemoheterotrophic conditions. Appl Microbiol Biotechnol. 2016;100:8901-12. https://doi.org/10.1007/s00253-016-7711-5.
McCully AL, Onyeziri MC, LaSarre B, Gliessman JR, McKinlay JB. Reductive tricarboxylic acid cycle enzymes and reductive amino acid synthesis pathways contribute to electron balance in a Rhodospirillum rubrum Calvin-cycle mutant. Microbiology. 2020;166:199-211. https://doi.org/10.1099/mic.0.000877.
Martin RR, Marshall VD, Sokatch JR, Unger L. Common enzymes of branched-chain amino acid catabolism in Pseudomonas putida. J Bacteriol. 1973;115:198-204. https://doi.org/10.1128/JB.115.1.198-204.1973.
Kazakov AE, Rodionov DA, Alm E, Arkin AP, Dubchak I, Gelfand MS. Comparative genomics of regulation of fatty acid and branched-chain amino acid utilization in proteobacteria. J Bacteriol. 2009;191:52-64. https://doi.org/10.1128/JB.01175-08.
Yamamoto H, Fang M, Dragnea V, Bauer CE. Differing isoforms of the cobalamin binding photoreceptor AerR oppositely regulate photosystem expression. Elife. 2018;7. https://doi.org/10.7554/eLife.39028.
Fang M, Bauer CE. Regulation of stringent factor by branched-chain amino acids. Proc Natl Acad Sci. 2018;115:6446-51. https://doi.org/10.1073/pnas.1803220115.
Ratnatilleke A, Vrijbloed JW, Robinson JA. Cloning and sequencing of the coenzyme B12-binding domain of isobutyryl-CoA mutase from Streptomyces cinnamonensis, reconstitution of mutase activity, and characterization of the recombinant enzyme produced in Escherichia coli. J Biol Chem. 1999;274:31679-85. https://doi.org/10.1074/jbc.274.44.31679.
Vrijbloed JW, Zerbe-Burkhardt K, Ratnatilleke A, Grubelnik-Leiser A, Robinson JA. Insertional inactivation of methylmalonyl coenzyme a (CoA) mutase and isobutyryl-CoA mutase genes in Streptomyces cinnamonensis: influence on polyketide antibiotic biosynthesis. J Bacteriol. 1999;181:5600-5. https://doi.org/10.1128/JB.181.18.5600-5605.1999.
Birch A, Leiser A, Robinson JA. Cloning, sequencing, and expression of the gene encoding methylmalonyl-coenzyme a mutase from Streptomyces cinnamonensis. J Bacteriol. 1993;175:3511-9. https://doi.org/10.1128/JB.175.11.3511-3519.1993.
Jost M, Born DA, Cracan V, Banerjee R, Drennan CL. Structural basis for substrate specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and related acyl-CoA Mutases. J Biol Chem. 2015;290:26882-98. https://doi.org/10.1074/jbc.M115.676890.
Massey LK, Conrad RS, Sokatch JR. Regulation of leucine catabolism in Pseudomonas putida. J Bacteriol. 1974;118:112-20. https://doi.org/10.1128/JB.118.1.112-120.1974.
Heider J, Mai X, Adams MW. Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea. J Bacteriol. 1996;178:780-7. https://doi.org/10.1128/JB.178.3.780-787.1996.
Mai X, Adams MW. Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J Bacteriol. 1996;178:5890-6. https://doi.org/10.1128/JB.178.20.5890-5896.1996.
Tersteegen A, Linder D, Thauer RK, Hedderich R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur J Biochem. 1997;244:862-8. https://doi.org/10.1111/j.1432-1033.1997.00862.x.
Story SV, Shah C, Jenney FE, Adams MWW. Characterization of a novel zinc-containing, lysine-specific Aminopeptidase from the Hyperthermophilic Archaeon Pyrococcus furiosus. J Bacteriol. 2005;187:2077-83. https://doi.org/10.1128/JB.187.6.2077-2083.2005.
Sznajder A, Jendrossek D. Biochemical characterization of a new type of intracellular PHB depolymerase from Rhodospirillum rubrum with high hydrolytic activity on native PHB granules. Appl Microbiol Biotechnol. 2011;89:1487-95. https://doi.org/10.1007/s00253-011-3096-7.
Ning C, Gest H. Regulation of L-isoleucine biosynthesis in the photosynthetic bacterium rhodospirillum rubrum. Proc Natl Acad Sci U S A. 1966;56:1823-7.
