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Rational engineering of Geobacter sulfurreducens electron transfer components: a foundation for building improved Geobacter-based bioelectrochemical technologies.

Frontiers in microbiology

Dantas JM, Morgado L, Aklujkar M, Bruix M, Londer YY, Schiffer M, Pokkuluri PR, Salgueiro CA.
PMID: 26284042
Front Microbiol. 2015 Jul 30;6:752. doi: 10.3389/fmicb.2015.00752. eCollection 2015.

Multiheme cytochromes have been implicated in Geobacter sulfurreducens extracellular electron transfer (EET). These proteins are potential targets to improve EET and enhance bioremediation and electrical current production by G. sulfurreducens. However, the functional characterization of multiheme cytochromes is particularly...

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Dantas JM, Morgado L, Aklujkar M, et al. Rational engineering of Geobacter sulfurreducens electron transfer components: a foundation for building improved Geobacter-based bioelectrochemical technologies. Front Microbiol. 2015;6:752doi: 10.3389/fmicb.2015.00752.
Dantas, J. M., Morgado, L., Aklujkar, M., Bruix, M., Londer, Y. Y., Schiffer, M., Pokkuluri, P. R., & Salgueiro, C. A. (2015). Rational engineering of Geobacter sulfurreducens electron transfer components: a foundation for building improved Geobacter-based bioelectrochemical technologies. Frontiers in microbiology, 6752. https://doi.org/10.3389/fmicb.2015.00752
Dantas, Joana M, et al. "Rational engineering of Geobacter sulfurreducens electron transfer components: a foundation for building improved Geobacter-based bioelectrochemical technologies." Frontiers in microbiology vol. 6 (2015): 752. doi: https://doi.org/10.3389/fmicb.2015.00752
Dantas JM, Morgado L, Aklujkar M, Bruix M, Londer YY, Schiffer M, Pokkuluri PR, Salgueiro CA. Rational engineering of Geobacter sulfurreducens electron transfer components: a foundation for building improved Geobacter-based bioelectrochemical technologies. Front Microbiol. 2015 Jul 30;6:752. doi: 10.3389/fmicb.2015.00752. eCollection 2015. PMID: 26284042; PMCID: PMC4519760.
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Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1.

Frontiers in microbiology

Alves MN, Neto SE, Alves AS, Fonseca BM, Carrêlo A, Pacheco I, Paquete CM, Soares CM, Louro RO.
PMID: 26175726
Front Microbiol. 2015 Jun 29;6:665. doi: 10.3389/fmicb.2015.00665. eCollection 2015.

The versatile anaerobic metabolism of the Gram-negative bacterium Shewanella oneidensis MR-1 (SOMR-1) relies on a multitude of redox proteins found in its periplasm. Most are multiheme cytochromes that carry electrons to terminal reductases of insoluble electron acceptors located at...

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Alves MN, Neto SE, Alves AS, et al. Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1. Front Microbiol. 2015;6:665doi: 10.3389/fmicb.2015.00665.
Alves, M. N., Neto, S. E., Alves, A. S., Fonseca, B. M., Carrêlo, A., Pacheco, I., Paquete, C. M., Soares, C. M., & Louro, R. O. (2015). Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1. Frontiers in microbiology, 6665. https://doi.org/10.3389/fmicb.2015.00665
Alves, Mónica N, et al. "Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1." Frontiers in microbiology vol. 6 (2015): 665. doi: https://doi.org/10.3389/fmicb.2015.00665
Alves MN, Neto SE, Alves AS, Fonseca BM, Carrêlo A, Pacheco I, Paquete CM, Soares CM, Louro RO. Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1. Front Microbiol. 2015 Jun 29;6:665. doi: 10.3389/fmicb.2015.00665. eCollection 2015. PMID: 26175726; PMCID: PMC4484225.
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Photo-oxidation of membrane-bound and soluble cytochromec in the green sulfur bacteriumChlorobium tepidum.

Photosynthesis research

Okumura N, Shimada K, Matsuura K.
PMID: 24310018
Photosynth Res. 1994 Jul;41(1):125-34. doi: 10.1007/BF02184152.

We studied the photosynthetic electron transfer system of membrane-bound and soluble cytochromec inChlorobium tepidum, a thermophilic green sulfur bacterium, using whole cells and membrane preparations. Sulfide and thiosulfate, physiological electron donors, enhanced flash-induced photo-oxidation ofc-type cytochromes in whole cells....

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Okumura N, Shimada K, Matsuura K. Photo-oxidation of membrane-bound and soluble cytochromec in the green sulfur bacteriumChlorobium tepidum. Photosynth Res. 1994;41(1):125-34doi: 10.1007/BF02184152.
Okumura, N., Shimada, K., & Matsuura, K. (1994). Photo-oxidation of membrane-bound and soluble cytochromec in the green sulfur bacteriumChlorobium tepidum. Photosynthesis research, 41(1), 125-34. https://doi.org/10.1007/BF02184152
Okumura, N, et al. "Photo-oxidation of membrane-bound and soluble cytochromec in the green sulfur bacteriumChlorobium tepidum." Photosynthesis research vol. 41,1 (1994): 125-34. doi: https://doi.org/10.1007/BF02184152
Okumura N, Shimada K, Matsuura K. Photo-oxidation of membrane-bound and soluble cytochromec in the green sulfur bacteriumChlorobium tepidum. Photosynth Res. 1994 Jul;41(1):125-34. doi: 10.1007/BF02184152. PMID: 24310018.
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Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea.

Environmental toxicology and pharmacology

Vidal M, Bassères A, Narbonne J.
PMID: 11167153
Environ Toxicol Pharmacol. 2001 Jan 01;9(3):87-97. doi: 10.1016/s1382-6689(00)00068-5.

Freshwater clams Corbicula fluminea were exposed in aquariums to four doses of trichloroethylene-TCE-(1.56 up to 100 mg/1) or toluene-TOL-(7.5 up to 60 mg/1) for 5 days. At the end of exposure, components of (de)toxification metabolism of phases I and...

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Vidal M, Bassères A, Narbonne J. Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea. Environ Toxicol Pharmacol. 2001;9(3):87-97doi: 10.1016/s1382-6689(00)00068-5.
Vidal, M., Bassères, A., & Narbonne, J. (2001). Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea. Environmental toxicology and pharmacology, 9(3), 87-97. https://doi.org/10.1016/s1382-6689(00)00068-5
Vidal, M -L., et al. "Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea." Environmental toxicology and pharmacology vol. 9,3 (2001): 87-97. doi: https://doi.org/10.1016/s1382-6689(00)00068-5
Vidal M, Bassères A, Narbonne J. Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea. Environ Toxicol Pharmacol. 2001 Jan 01;9(3):87-97. doi: 10.1016/s1382-6689(00)00068-5. PMID: 11167153.
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[No title available]

FEBS letters

Verdière J, Lederer F.
PMID: 11946178
FEBS Lett. 1971 Nov 15;19(1):72-74. doi: 10.1016/0014-5793(71)80608-7.

It is shown that the iso-1 and iso-2 cytochromes c synthesized by two strains of respiratory deficient strains of yeast (varrho(-)) possess one residue of epsilonN-trimethyllysine and do not differ in this respect from the iso-cytochromes produced by varrho(+)...

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Verdière J, Lederer F. Présence de la epsilonN-trimethyllysine dans l'iso-1 et l'iso-2 cytochromes c synthétisés par des souches de levure à déficience respiratoire (varrho(-)). . FEBS Lett. 1971;19(1):72-74doi: 10.1016/0014-5793(71)80608-7.
Verdière, J., & Lederer, F. (1971). Présence de la epsilonN-trimethyllysine dans l'iso-1 et l'iso-2 cytochromes c synthétisés par des souches de levure à déficience respiratoire (varrho(-)). . FEBS letters, 19(1), 72-74. https://doi.org/10.1016/0014-5793(71)80608-7
Verdière, J, and Lederer, F. "Présence de la epsilonN-trimethyllysine dans l'iso-1 et l'iso-2 cytochromes c synthétisés par des souches de levure à déficience respiratoire (varrho(-))." . FEBS letters vol. 19,1 (1971): 72-74. doi: https://doi.org/10.1016/0014-5793(71)80608-7
Verdière J, Lederer F. Présence de la epsilonN-trimethyllysine dans l'iso-1 et l'iso-2 cytochromes c synthétisés par des souches de levure à déficience respiratoire (varrho(-)). . FEBS Lett. 1971 Nov 15;19(1):72-74. doi: 10.1016/0014-5793(71)80608-7. French. PMID: 11946178.
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Enzyme-catalyzed processes of first-pass hepatic and intestinal drug extraction.

Advanced drug delivery reviews

Shen DD, Kunze KL, Thummel KE.
PMID: 10837554
Adv Drug Deliv Rev. 1997 Sep 15;27(2):99-127. doi: 10.1016/s0169-409x(97)00039-2.

Oral bioavailability of pharmacologically effective drugs is often limited by first-pass biotransformation. In humans, both hepatic and intestinal enzymes can catalyze the metabolism of a drug as it transits between the gastrointestinal lumen and systemic blood for the first...

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Shen DD, Kunze KL, Thummel KE. Enzyme-catalyzed processes of first-pass hepatic and intestinal drug extraction. Adv Drug Deliv Rev. 1997;27(2):99-127doi: 10.1016/s0169-409x(97)00039-2.
Shen, D. D., Kunze, K. L., & Thummel, K. E. (1997). Enzyme-catalyzed processes of first-pass hepatic and intestinal drug extraction. Advanced drug delivery reviews, 27(2), 99-127. https://doi.org/10.1016/s0169-409x(97)00039-2
Shen, et al. "Enzyme-catalyzed processes of first-pass hepatic and intestinal drug extraction." Advanced drug delivery reviews vol. 27,2 (1997): 99-127. doi: https://doi.org/10.1016/s0169-409x(97)00039-2
Shen DD, Kunze KL, Thummel KE. Enzyme-catalyzed processes of first-pass hepatic and intestinal drug extraction. Adv Drug Deliv Rev. 1997 Sep 15;27(2):99-127. doi: 10.1016/s0169-409x(97)00039-2. PMID: 10837554.
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Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases.

Plant physiology

Van Gestelen P, Asard H, Caubergs RJ.
PMID: 12223822
Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543.

Solubilization and ion-exchange chromatography of plasma membrane proteins obtained from bean (Phaseolus vulgaris L.) seedlings resulted in a single NAD(P)H-O2--synthase protein peak. This enzyme showed a high preference toward NADPH as a substrate (reaction rate, 27.4 nmol O2- produced...

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Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997;115(2):543-550doi: 10.1104/pp.115.2.543.
Van Gestelen, P., Asard, H., & Caubergs, R. J. (1997). Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant physiology, 115(2), 543-550. https://doi.org/10.1104/pp.115.2.543
Van Gestelen, P., et al. "Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases." Plant physiology vol. 115,2 (1997): 543-550. doi: https://doi.org/10.1104/pp.115.2.543
Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543. PMID: 12223822; PMCID: PMC158513.
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PHOTOSYNTHETIC CYTOCHROMES c IN CYANOBACTERIA, ALGAE, AND PLANTS.

Annual review of plant physiology and plant molecular biology

Kerfeld CA, Krogmann DW.
PMID: 15012240
Annu Rev Plant Physiol Plant Mol Biol. 1998 Jun;49:397-425. doi: 10.1146/annurev.arplant.49.1.397.

The cytochromes that function in photosynthesis in cyanobacteria, algae, and higher plants have, like the other photosynthetic catalysts, been largely conserved in their structure and function during evolution. Cyanobacteria and algae contain cytochrome c6, which is not found in...

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Kerfeld CA, Krogmann DW. PHOTOSYNTHETIC CYTOCHROMES c IN CYANOBACTERIA, ALGAE, AND PLANTS. Annu Rev Plant Physiol Plant Mol Biol. 1998;49:397-425doi: 10.1146/annurev.arplant.49.1.397.
Kerfeld, C. A., & Krogmann, D. W. (1998). PHOTOSYNTHETIC CYTOCHROMES c IN CYANOBACTERIA, ALGAE, AND PLANTS. Annual review of plant physiology and plant molecular biology, 49397-425. https://doi.org/10.1146/annurev.arplant.49.1.397
Kerfeld, Cheryl A., and Krogmann, David W.. "PHOTOSYNTHETIC CYTOCHROMES c IN CYANOBACTERIA, ALGAE, AND PLANTS." Annual review of plant physiology and plant molecular biology vol. 49 (1998): 397-425. doi: https://doi.org/10.1146/annurev.arplant.49.1.397
Kerfeld CA, Krogmann DW. PHOTOSYNTHETIC CYTOCHROMES c IN CYANOBACTERIA, ALGAE, AND PLANTS. Annu Rev Plant Physiol Plant Mol Biol. 1998 Jun;49:397-425. doi: 10.1146/annurev.arplant.49.1.397. PMID: 15012240.
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[No title available]

FEBS letters

Gürtler L, Horstmann HJ.
PMID: 11946095
FEBS Lett. 1971 Oct 15;18(1):106-108. doi: 10.1016/0014-5793(71)80419-2.

Cytochrome c of the zebra (Equus guagga Boehmi) differs from horse cytochrome c in having in its polypeptide chain one serine residue instead of none and 9 threonine residues instead of 10. This replacement has been localised at position...

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Gürtler L, Horstmann HJ. Zur primärstruktur des cytochromes c des steppenzebras (Equus quagga Boehmi). . FEBS Lett. 1971;18(1):106-108doi: 10.1016/0014-5793(71)80419-2.
Gürtler, L., & Horstmann, H. J. (1971). Zur primärstruktur des cytochromes c des steppenzebras (Equus quagga Boehmi). . FEBS letters, 18(1), 106-108. https://doi.org/10.1016/0014-5793(71)80419-2
Gürtler, L, and Horstmann, H J.. "Zur primärstruktur des cytochromes c des steppenzebras (Equus quagga Boehmi)." . FEBS letters vol. 18,1 (1971): 106-108. doi: https://doi.org/10.1016/0014-5793(71)80419-2
Gürtler L, Horstmann HJ. Zur primärstruktur des cytochromes c des steppenzebras (Equus quagga Boehmi). . FEBS Lett. 1971 Oct 15;18(1):106-108. doi: 10.1016/0014-5793(71)80419-2. German. PMID: 11946095.
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Etiolated cells of Chlamydomonas reinhardtii: choice material for characterization of mitochondrial membrane polypeptides.

Proceedings of the National Academy of Sciences of the United States of America

Bennoun P, Atteia A, Pierre Y, Delosme M.
PMID: 11607585
Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10202-6. doi: 10.1073/pnas.92.22.10202.

We have investigated a light-conditional mutant of Chlamydomonas reinhardtii (J12) that is unable to synthesize chlorophyll in the dark with the aim of characterizing the mitochondrial membrane polypeptides of this alga. A crude membrane fraction derived from etiolated cells...

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Bennoun P, Atteia A, Pierre Y, et al. Etiolated cells of Chlamydomonas reinhardtii: choice material for characterization of mitochondrial membrane polypeptides. Proc Natl Acad Sci U S A. 1995;92(22):10202-6doi: 10.1073/pnas.92.22.10202.
Bennoun, P., Atteia, A., Pierre, Y., & Delosme, M. (1995). Etiolated cells of Chlamydomonas reinhardtii: choice material for characterization of mitochondrial membrane polypeptides. Proceedings of the National Academy of Sciences of the United States of America, 92(22), 10202-6. https://doi.org/10.1073/pnas.92.22.10202
Bennoun, P, et al. "Etiolated cells of Chlamydomonas reinhardtii: choice material for characterization of mitochondrial membrane polypeptides." Proceedings of the National Academy of Sciences of the United States of America vol. 92,22 (1995): 10202-6. doi: https://doi.org/10.1073/pnas.92.22.10202
Bennoun P, Atteia A, Pierre Y, Delosme M. Etiolated cells of Chlamydomonas reinhardtii: choice material for characterization of mitochondrial membrane polypeptides. Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10202-6. doi: 10.1073/pnas.92.22.10202. PMID: 11607585; PMCID: PMC40764.
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Thermodynamics of the redox reaction of cytochromes c of five different species.

FEBS letters

Margalit R, Schejter A.
PMID: 11947394
FEBS Lett. 1970 Feb 16;6(3):278-280. doi: 10.1016/0014-5793(70)80077-1.

No abstract available.

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Margalit R, Schejter A. Thermodynamics of the redox reaction of cytochromes c of five different species. FEBS Lett. 1970;6(3):278-280doi: 10.1016/0014-5793(70)80077-1.
Margalit, R., & Schejter, A. (1970). Thermodynamics of the redox reaction of cytochromes c of five different species. FEBS letters, 6(3), 278-280. https://doi.org/10.1016/0014-5793(70)80077-1
Margalit, R, and Schejter, A. "Thermodynamics of the redox reaction of cytochromes c of five different species." FEBS letters vol. 6,3 (1970): 278-280. doi: https://doi.org/10.1016/0014-5793(70)80077-1
Margalit R, Schejter A. Thermodynamics of the redox reaction of cytochromes c of five different species. FEBS Lett. 1970 Feb 16;6(3):278-280. doi: 10.1016/0014-5793(70)80077-1. PMID: 11947394.
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Redox transitions of cytochromes and pyridine nucleotides upon stimulation of an isolated rat ganglion.

FEBS letters

Brauser B, Bücher T, Dolivo M.
PMID: 11947598
FEBS Lett. 1970 Jun 27;8(5):297-300. doi: 10.1016/0014-5793(70)80291-5.

No abstract available.

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Brauser B, Bücher T, Dolivo M. Redox transitions of cytochromes and pyridine nucleotides upon stimulation of an isolated rat ganglion. FEBS Lett. 1970;8(5):297-300doi: 10.1016/0014-5793(70)80291-5.
Brauser, B., Bücher, T., & Dolivo, M. (1970). Redox transitions of cytochromes and pyridine nucleotides upon stimulation of an isolated rat ganglion. FEBS letters, 8(5), 297-300. https://doi.org/10.1016/0014-5793(70)80291-5
Brauser, B, et al. "Redox transitions of cytochromes and pyridine nucleotides upon stimulation of an isolated rat ganglion." FEBS letters vol. 8,5 (1970): 297-300. doi: https://doi.org/10.1016/0014-5793(70)80291-5
Brauser B, Bücher T, Dolivo M. Redox transitions of cytochromes and pyridine nucleotides upon stimulation of an isolated rat ganglion. FEBS Lett. 1970 Jun 27;8(5):297-300. doi: 10.1016/0014-5793(70)80291-5. PMID: 11947598.
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Showing 13 to 24 of 514 entries