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1962 1
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2010 19
2011 12
2012 19
2013 18
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369 results

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Page 1
Mitochondrial complex I.
Hirst J. Hirst J. Annu Rev Biochem. 2013;82:551-75. doi: 10.1146/annurev-biochem-070511-103700. Epub 2013 Mar 18. Annu Rev Biochem. 2013. PMID: 23527692 Review.
Complex I (NADH:ubiquinone oxidoreductase) is crucial for respiration in many aerobic organisms. In mitochondria, it oxidizes NADH from the tricarboxylic acid cycle and beta-oxidation, reduces ubiquinone, and transports protons across the inner membrane, cont …
Complex I (NADH:ubiquinone oxidoreductase) is crucial for respiration in many aerobic organisms. In mitochondria, it oxidizes …
Quinoprotein-catalysed reactions.
Anthony C. Anthony C. Biochem J. 1996 Dec 15;320 ( Pt 3)(Pt 3):697-711. doi: 10.1042/bj3200697. Biochem J. 1996. PMID: 9003352 Free PMC article. Review.
These have prosthetic groups containing quinones, the name thus being analogous to the flavoproteins containing flavin prosthetic groups. Pyrrolo-quinoline quinone (PQQ) is non-covalently attached, whereas tryptophan tryptophylquinone (TTQ), topaquinone (TPQ) and ly …
These have prosthetic groups containing quinones, the name thus being analogous to the flavoproteins containing flavin prosthe …
Flavin-dependent quinone reductases.
Deller S, Macheroux P, Sollner S. Deller S, et al. Cell Mol Life Sci. 2008 Jan;65(1):141-60. doi: 10.1007/s00018-007-7300-y. Cell Mol Life Sci. 2008. PMID: 17938860 Free PMC article. Review.
Several species have been shown to possess enzymes that afford the two-electron reduction to the hydroquinone form in an attempt to avoid the generation of one-electron reduced semiquinone known to cause oxidative stress. These enzymes utilize a flavin …
Several species have been shown to possess enzymes that afford the two-electron reduction to the hydroquinone form in an attempt to a …
Regulated methionine oxidation by monooxygenases.
Manta B, Gladyshev VN. Manta B, et al. Free Radic Biol Med. 2017 Aug;109:141-155. doi: 10.1016/j.freeradbiomed.2017.02.010. Epub 2017 Feb 14. Free Radic Biol Med. 2017. PMID: 28229915 Free PMC article. Review.
Redox-dependent regulatory mechanisms have been identified for nearly every cellular process, but the major paradigm has been that cellular components are oxidized (damaged) by reactive oxygen species (ROS) in a relatively unspecific way, and then reduced (repaired) …
Redox-dependent regulatory mechanisms have been identified for nearly every cellular process, but the major paradigm has been that cellular …
Multidomain flavin-dependent sulfhydryl oxidases.
Coppock DL, Thorpe C. Coppock DL, et al. Antioxid Redox Signal. 2006 Mar-Apr;8(3-4):300-11. doi: 10.1089/ars.2006.8.300. Antioxid Redox Signal. 2006. PMID: 16677076 Review.
Eukaryotic flavin-dependent sulfhydryl oxidases catalyze oxidative protein folding with the generation of disulfides and the reduction of oxygen to hydrogen peroxide. ...Interdomain disulfide exchanges transmit reducing equivalents from substrates to t …
Eukaryotic flavin-dependent sulfhydryl oxidases catalyze oxidative protein folding with the generation of disulfides and the reduc …
Structure of human phagocyte NADPH oxidase in the activated state.
Liu X, Shi Y, Liu R, Song K, Chen L. Liu X, et al. Nature. 2024 Mar;627(8002):189-195. doi: 10.1038/s41586-024-07056-1. Epub 2024 Feb 14. Nature. 2024. PMID: 38355798
However, the exact mechanism by which cytosolic factors bind to and activate NOX2 is not well understood. Here we present the structure of the human NOX2-p22 complex activated by fragments of three cytosolic factors: p47, p67 and Rac1. The structure reveals that the …
However, the exact mechanism by which cytosolic factors bind to and activate NOX2 is not well understood. Here we present the structu …
The FMN-dependent two-component monooxygenase systems.
Ellis HR. Ellis HR. Arch Biochem Biophys. 2010 May;497(1-2):1-12. doi: 10.1016/j.abb.2010.02.007. Epub 2010 Mar 1. Arch Biochem Biophys. 2010. PMID: 20193654 Review.
The role of the reductase is to supply reduced flavin to the monooxygenase enzyme, while the monooxygenase enzyme utilizes the reduced flavin to activate molecular oxygen. ...An interesting feature of these enzymes is their ability …
The role of the reductase is to supply reduced flavin to the monooxygenase enzyme, while the monooxygenase enzyme utilizes the …
How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis.
Imlay JA. Imlay JA. Adv Microb Physiol. 2002;46:111-53. doi: 10.1016/s0065-2911(02)46003-1. Adv Microb Physiol. 2002. PMID: 12073652 Review.
The orbital structure of molecular oxygen constrains it to accept electrons one at a time, and its unfavourable univalent reduction potential ensures that it can do so only with low-potential redox partners. In E. coli, this restriction prevents oxy …
The orbital structure of molecular oxygen constrains it to accept electrons one at a time, and its unfavourable univale …
Activity coupling and complex formation between bacterial luciferase and flavin reductases.
Tu SC. Tu SC. Photochem Photobiol Sci. 2008 Feb;7(2):183-8. doi: 10.1039/b713462b. Epub 2007 Dec 20. Photochem Photobiol Sci. 2008. PMID: 18264585 Review.
Luminous bacteria contain several species of flavin reductases, which catalyze the reduction of FMN using NADH and/or NADPH as a reductant. The reduced FMN (i.e. FMNH(2)) so generated is utilized along with a long-chain aliphatic aldehyde and molecular …
Luminous bacteria contain several species of flavin reductases, which catalyze the reduction of FMN using NADH and/or NADPH as …
Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I.
Hirst J, Roessler MM. Hirst J, et al. Biochim Biophys Acta. 2016 Jul;1857(7):872-83. doi: 10.1016/j.bbabio.2015.12.009. Epub 2015 Dec 22. Biochim Biophys Acta. 2016. PMID: 26721206 Free PMC article. Review.
Complex I (NADH:ubiquinone oxidoreductase) is critical for respiration in mammalian mitochondria. It oxidizes NADH produced by the Krebs' tricarboxylic acid cycle and beta-oxidation of fatty acids, reduces ubiquinone, and transports protons to contribute to t …
Complex I (NADH:ubiquinone oxidoreductase) is critical for respiration in mammalian mitochondria. It oxidizes NADH produced by …
369 results