DOI: 10.1128/jb.114.2.767-771.1973. Enzyme Complex Which Couples Glycerol-3-Phosphate Dehydrogenation to Fumarate Reduction in <i>Escherichia coli</i>

Enzyme Complex Which Couples Glycerol-3-Phosphate Dehydrogenation to Fumarate Reduction in Escherichia coli

10.1128/jb.114.2.767-771.1973

Crossref journal-article

American Society for Microbiology

Journal of Bacteriology (235)

Abstract

Anaerobic growth of Escherichia coli on glycerol as carbon source and fumarate as hydrogen acceptor results in the induction of both anaerobic sn -glycerol-3-phosphate (G3P) dehydrogenase and fumarate reductase. In previous studies, the G3P dehydrogenase was measured by the G3P-dependent reduction of a tetrazolium dye mediated by phenazine methosulfate in the presence of flavine mononucleotide and flavine adenine dinucleotide, and fumarate reductase was measured by the fumarate-dependent oxidation of reduced flavine mononucleotide. Results from the present study indicate that these two enzymes actually constitute a functional complex which is sedimentable at 200,000 × g in 2 h and which can catalyze the dehydrogenation of G3P at the expense of fumarate without any added cofactor. This coupling activity is not constituted by simply mixing an extract containing anaerobic G3P dehydrogenase with another extract containing fumarate reductase. Additional evidence for an organized complex is provided by the high degree of sensitivity of the coupled reaction to low concentrations of the detergents Triton X-100 and Emasol 1130 in comparison with the individual activities of the two component enzymes measured with the aid of artificial cofactors.

Bibliography

Miki, K., & Lin, E. C. C. (1973). Enzyme Complex Which Couples Glycerol-3-Phosphate Dehydrogenation to Fumarate Reduction in Escherichia coli. Journal of Bacteriology, 114(2), 767â771.

Authors 2

K. Miki (first)
E. C. C. Lin (additional)

References 14 Referenced 28

Cozzarelli , N. R. , W. B. Freedberg , and E. C. C. Lin . 1968 . Genetic control of the L-a-glycerophosphate system in Escherichia coli . J. Mol. Biol. 31 : 371 - 387 . (10.1016/0022-2836(68)90415-4) / J. Mol. Biol. / Genetic control of the L-a-glycerophosphate system in Escherichia coli by Cozzarelli N. R. (1968)
Faust , P. J. , and P. J. Vandemark . 1970 . Phosphorylation coupled to NADH oxidation with fumarate in Streptococcus faecalis 10Cl . Arch. Biochem. Biophys. 137 : 392 - 398 . (10.1016/0003-9861(70)90454-6) / Arch. Biochem. Biophys. / Phosphorylation coupled to NADH oxidation with fumarate in Streptococcus faecalis 10Cl by Faust P. J. (1970)
Gest , H. 1954 . Oxidation and evolution of molecular hydrogen by microorganisms . Bacteriol. Rev. 18 : 43 - 73 . (10.1128/BR.18.1.43-73.1954) / Bacteriol. Rev. / Oxidation and evolution of molecular hydrogen by microorganisms by Gest H. (1954)
Hatchikian , E. C. , and J. Le Gall . 1972 . Evidence for the presence of a b-type cytochrome in the sulfate-reducing bacterium Desulfovibrio gigas, and its role in the reduction of fumarate by molecular hydrogen . Biochim. Biophys. Acta 267 : 479 - 484 . (10.1016/0005-2728(72)90175-2) / Biochim. Biophys. Acta / Evidence for the presence of a b-type cytochrome in the sulfate-reducing bacterium Desulfovibrio gigas, and its role in the reduction of fumarate by molecular hydrogen by Hatchikian E. C. (1972)
Hayashi , S. , J. P. Koch , and E. C. C. Lin . 1964 . Active transport of L-a-glycerophosphate in Escherichia coli . J. Biol. Chem. 239 : 3098 - 3105 . (10.1016/S0021-9258(18)93858-5) / J. Biol. Chem. / Active transport of L-a-glycerophosphate in Escherichia coli by Hayashi S. (1964)
Hirsch , C. A. , M. Rasminsky , B. D. Davis , and E. C. C. Lin . 1963 . A fumarate reductase in Escherichia coli distinct from succinate dehydrogenase . J. Biol. Chem. 238-3770-3774. / J. Biol. Chem. 238-3770-3774. / A fumarate reductase in Escherichia coli distinct from succinate dehydrogenase by Hirsch C. A. (1963)
Hirschmann , H. 1960 . The nature of substrate asymmetry in stereoselective reactions . J. Biol. Chem. 235 : 2762 - 2767 . (10.1016/S0021-9258(18)64537-5) / J. Biol. Chem. / The nature of substrate asymmetry in stereoselective reactions by Hirschmann H. (1960)
Kistler , W. S. , and E. C. C. Lin . 1971 . Anaerobic L-a-glycerophosphate dehydrogenase of Escherichia coli: its genetic locus and its physiological role . J. Bacteriol. 108 : 1224 - 1234 . (10.1128/JB.108.3.1224-1234.1971) / J. Bacteriol. / Anaerobic L-a-glycerophosphate dehydrogenase of Escherichia coli: its genetic locus and its physiological role by Kistler W. S. (1971)
Kistler , W. S. , and E. C. C. Lin . 1972 . Purification and properties of the flavine-stimulated anaerobic L-aglycerophosphate of Escherichia coli . J. Bacteriol. 112 : 539 - 547 . (10.1128/JB.112.1.539-547.1972) / J. Bacteriol. / Purification and properties of the flavine-stimulated anaerobic L-aglycerophosphate of Escherichia coli by Kistler W. S. (1972)
Lowry , 0. H. , N. J. Rosebrough , A. L. Farr , and R. J. Randall . 1951 . Protein measurement with the Folin phenol reagent . J. Biol. Chem. 193 : 265 - 275 . (10.1016/S0021-9258(19)52451-6) / J. Biol. Chem. / Protein measurement with the Folin phenol reagent by Lowry 0. (1951)
Peck , H. D. , Jr. , 0. H. Smith , and H. Gest . 1957 . Comparative biochemistry of the biological reduction of fumaric acid . Biochim. Biophys. Acta 25 : 142 - 147 . (10.1016/0006-3002(57)90431-6) / Biochim. Biophys. Acta / Comparative biochemistry of the biological reduction of fumaric acid by Peck H. D. (1957)
Quastel , J. H. , and M. Stephenson . 1925 . Further observations on the anaerobic growth of bacteria . Biochem. J. 19 : 660 - 666 . (10.1042/bj0190660) / Biochem. J. / Further observations on the anaerobic growth of bacteria by Quastel J. H. (1925)
Quastel , J. H. , M. Stephenson , and M. D. Whetham . 1925 . Some reactions of resting bacteria in relation to anaerobic growth . Biochem. J. 19 : 304 - 317 . (10.1042/bj0190304) / Biochem. J. / Some reactions of resting bacteria in relation to anaerobic growth by Quastel J. H. (1925)
Tanaka , S. , S. A. Lerner , and E. C. C. Lin . 1967 . Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol . J. Bacteriol. 93 : 642 - 648 . (10.1128/JB.93.2.642-648.1967) / J. Bacteriol. / Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol by Tanaka S. (1967)

Dates

Type	When
Created	5 years, 8 months ago (Jan. 3, 2020, 9:42 a.m.)
Deposited	4 years, 1 month ago (July 29, 2021, 1:08 p.m.)
Indexed	1 year, 7 months ago (Jan. 18, 2024, 12:22 a.m.)
Issued	52 years, 4 months ago (May 1, 1973)
Published	52 years, 4 months ago (May 1, 1973)
Published Print	52 years, 4 months ago (May 1, 1973)

Funders 0

None

BibTeX

@article{Miki_1973, title={Enzyme Complex Which Couples Glycerol-3-Phosphate Dehydrogenation to Fumarate Reduction in Escherichia coli}, volume={114}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.114.2.767-771.1973}, DOI={10.1128/jb.114.2.767-771.1973}, number={2}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Miki, K. and Lin, E. C. C.}, year={1973}, month=may, pages={767–771} }

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