Podcasts about Cytochrome

Play Episode Listen Later Nov 3, 2020

Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.11.03.367284v1?rss=1 Authors: Brittain, T. J., O'Malley, M. C., Swaim, C. M., Fink, R. A., Kokhan, O. Abstract: C-type cytochromes play an important role in respiration of dissimilatory metal-reducing bacteria. They form extended conduits for charge transfer between the cellular metabolism and external electron acceptors such as particles of iron oxide, metal ions, and humic substances. Out of more than a hundred c-type cytochromes in Geobacter sulfurreducens, only a small fraction has been previously characterized. Here we present our results on expression and biophysical characterization of GSU0105, a novel 3-heme cytochrome, important for Fe(III) respiration in G. sulfurreducens. We successfully cloned the gene and achieved ~3 mg/L of culture GSU0105 expression in E.coli. Despite a similar size (71 amino acids) and the same number of c-type hemes to the members of the cytochrome (cyt) c7 family, multiple sequence alignment suggests that GSU0105 does not belong to the cyt c7 family. UV-Vis spectroscopy revealed typical c-type cytochrome spectral features, including a weak iron-sulfur charge transfer band suggesting that at least one heme is ligated with a methionine residue. Far UV circular dichroism studies demonstrate approximately 35% content of -helices and {beta}-sheets, each, as well as thermal aggregation occurring above 60C. A combination of SAXS and analytical size exclusion chromatography data shows that GSU0105 is monomeric in solution. Finally, affinity pull-down assays demonstrate high binding affinity to PpcD and weaker binding to the other members of the cyt c7 family. Copy rights belong to original authors. Visit the link for more info

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Heme oxygenase-1 affects cytochrome P450 function through the formation of heteromeric complexes: Interactions between CYP1A2 and heme oxygenase-1

Play Episode Listen Later Sep 14, 2020

Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.09.14.296467v1?rss=1 Authors: Connick, J. P., Reed, J. R., Cawley, G. F., Backes, W. L. Abstract: Heme oxygenase 1 (HO-1) and the cytochromes P450 (P450s) are endoplasmic reticulum-bound enzymes that rely on the same protein, NADPH-cytochrome P450 reductase (POR), to provide the electrons necessary for substrate metabolism. Although the HO-1 and P450 systems are interconnected due to their common electron donor, they generally have been studied separately. As the expression of both HO-1 and P450s are affected by xenobiotic exposure, changes in HO-1 expression can potentially affect P450 function, and conversely, changes in P450 expression can influence HO-1. The goal of this study was to examine interactions between the P450 and HO-1 systems. Using bioluminescence resonance energy transfer (BRET), HO-1 formed HO-1P450 complexes with CYP1A2, CYP1A1, and CYP2D6, but not all P450s. Studies then focused on the HO-1/CYP1A2 interaction. CYP1A2 formed a physical complex with HO-1 that was stable in the presence of POR. As expected, both HO-1 and CYP1A2 formed BRET-detectable complexes with POR. Whereas the PORCYP1A2 complex was readily disrupted by the addition of HO-1, the PORHO-1 complex was not significantly affected by the addition of CYP1A2. Interestingly, enzyme activities did not follow this pattern. Whereas BRET data suggested substantial inhibition of CYP1A2-mediated 7-ethoxyresorufin deethylation in the presence of HO-1, its activity was actually stimulated at subsaturating POR. In contrast, HO-1-mediated heme metabolism was inhibited at subsaturating POR. These results indicate that HO-1 and CYP1A2 form a stable complex and have mutual effects on the catalytic behavior of both proteins that cannot be explained by simple competition for POR. Copy rights belong to original authors. Visit the link for more info

studies copy formation function bret interactions complexes cawley heme backes biorxiv p450 nadph cytochrome cyp1a2 cyp2d6

Two bi-functional cytochrome P450 CYP72 enzymes from olive (Olea europaea) catalyze the oxidative C-C bond cleavage in the biosynthesis of secoxy-iridoids - flavor and quality determinants in olive oil

Play Episode Listen Later Aug 28, 2020

Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.08.28.265934v1?rss=1 Authors: Rodriguez-Lopez, C. E., Hong, B., Paetz, C., Nakamura, Y., Koudounas, K., Passeri, V., Baldoni, L., Alagna, F., Calderini, O., O'Connor, S. E. Abstract: Olive (Olea europaea) is an important crop in Europe, with high cultural, economic, and nutritional significance. Olive oil flavor and quality depend on phenolic secoiridoids, but the biosynthetic pathway of these iridoids remains largely uncharacterized. We discovered two novel, bi-functional cytochrome P450 enzymes, catalysing the rare oxidative C-C bond cleavage of 7-epi-loganin to produce oleoside methyl ester (OeOMES) and secoxyloganin (OeSXS), both through a ketologanin intermediary. Although these enzymes are homologous to the previously reported Catharanthus roseus Secologanin Synthase (CrSLS), the substrate and product profiles differ. Biochemical assays provided mechanistic insights into the two-step OeOMES and CrSLS reactions. Model-guided mutations of OeOMES changed the product profile in a predictable manner, revealing insights into the molecular basis for this change in product specificity. Our results suggest that, in contrast to published hypotheses, in planta production of secoxy-iridoids is secologanin independent. Notably, sequence data of cultivated and wild olives, points to a relation between domestication and OeOMES expression. Thus, the discovery of this key biosynthetic gene suggests a link between domestication and secondary metabolism, and could potentially be used as a genetic marker to guide next-generation breeding programs. Copy rights belong to original authors. Visit the link for more info

Hydroxylation of antitubercular drug candidate, SQ109, by mycobacterial cytochrome P450

healthy myth diet debunking utilizing uv carbs carbohydrates cytochrome

Play Episode Listen Later Aug 27, 2020

Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.08.27.269936v1?rss=1 Authors: Bukhdruker, S., Varaksa, T., Grabovec, I., Marin, E., Shabunya, P., Kadukova, M., Grudinin, S., Kavaleuski, A., Gusach, A., Gilep, A., Borshchevskiy, V., Strushkevich, N. Abstract: Spreading of the multidrug-resistant (MDR) strains of the deadliest pathogen Mycobacterium tuberculosis (Mtb) generates the need for new effective drugs. SQ109 showed activity against resistant Mtb and already advanced to Phase II/III clinical trials. Fast SQ109 degradation is attributed to the human liver Cytochrome P450s (CYPs). However, no information is available about interactions of the drug with Mtb CYPs. Here, we show that Mtb CYP124, previously assigned as a methyl-branched lipid monooxygenase, binds and hydroxylates SQ109 in vitro. A 1.25-[A] resolution crystal structure of the CYP124-SQ109 complex unambiguously shows two conformations of the drug, both positioned for hydroxylation of the {omega}-methyl group in the trans position. The hydroxylated SQ109 presumably forms stabilizing H-bonds with its target, i.e., the Mycobacterial membrane protein Large 3 (MmpL3). We anticipate that Mtb CYPs could function as analogs of drug-metabolizing human CYPs affecting pharmacokinetics and pharmacodynamics of antitubercular (anti-TB) drugs. Copy rights belong to original authors. Visit the link for more info

large drug candidate copy tb mtb mdr mycobacterium biorxiv p450 cytochrome mycobacterial

Methylene Blue: Part 1 with Dr. Francisco Gonzalez-Lima

Decoding Superhuman

Play Episode Listen Later Aug 25, 2020 49:03

Dr. Francisco Gonzalez-Lima is one of the world's leading neuroscientists and an expert in Cytochrome Oxidase. This is part one of a two part discussion. Dr. Gonzalez-Lima educates on the role of cytochrome oxidase and the history of methylene blue. Who is Dr. Francisco Gonzalez-Lima? Francisco Gonzalez-Lima, Ph.D., is a courtesy professor in the Department of Psychiatry. He also holds the George I. Sanchez Centennial Professorship at The University of Texas at Austin, where he is a professor in the departments of Psychology, Psychiatry, Pharmacology and Toxicology and the Institute for Neuroscience.Gonzalez-Lima’s teaching experience includes undergraduate, medical, graduate and postdoctoral students, and he currently teaches the core graduate course in Functional Neuroanatomy. Gonzalez-Lima has been the research adviser of 22 Ph.D. students at UT Austin, and his trainees are world leaders in brain research on the relationship between brain energy metabolism, memory and neurobehavioral disorders.Gonzalez-Lima graduated with honors from Tulane University in New Orleans with a Bachelor of Science in biology and Bachelor of Arts in psychology, and he earned his doctorate in anatomy and neurobiology from the University of Puerto Rico School of Medicine, which honored him with a Distinguished Alumnus Award. He completed postdoctoral training (behavioral neuroscience) at the Technical University of Darmstadt, Germany, as an Alexander von Humboldt research fellow.Gonzalez-Lima has been a visiting neuroscientist in Germany, England, Canada and Spain and he has delivered more than 120 invited lectures about his brain research around the world. His research has been funded for more than 30 years with federal and private funds, and he has contributed to more than 350 scientific publications in peer-reviewed journals, conference proceedings, chapters and books.Current research in the Gonzalez-Lima laboratory focuses on the beneficial neurocognitive and emotional effects of noninvasive human brain stimulation in healthy, aging and mentally ill populations. This research primarily uses transcranial infrared laser stimulation and multimodal imaging (EEG, fNIRS and fMRI) in collaboration with colleagues at UT Austin, The University of Texas at Arlington and University of Texas Southwestern Medical Center. Gonzalez-Lima supervises and trains students and residents to contribute to these ongoing brain research projects.Highlights[17:13] Cytochrome oxidase as a marker for longevity[25:14] Dr. Gonzalez-Lima's journey into methylene blue[37:20] What is the history of methylene blue?[39:40] Magic Bullet[44:36] Methylene Blue dosingResourcesMethylene Blue Preserves Cytochrome Oxidase Activity and Prevents Neurodegeneration and Memory Impairment in Rats With Chronic Cerebral HypoperfusionEnergy hypometabolism in posterior cingulate cortex of Alzheimer's patients: superficial laminar cytochrome oxidase associated with disease durationPaul EhrlichSponsorsBlue Cannatine One of my favorite tools for cognitive enhancement, especially after long plan rides, is Blue Cannatine. The delivery mechanism is unique (buccle troche). It is especially effective for me on improving short-term memory, focus, and verbal fluency.It’s the closest thing that I found to NZT and I think you guys should try it out. Get yours at troscriptions.com.Full disclosure: I am involved with the company (I like the product that much).BiOptimizers If you’re over 35, your enzyme levels have already begun to decline and your immune system can be more susceptible to viruses.Enzymes are the workhorses of digestion. They break your food down into usable macro and micronutrients. Research shows that by the time someone hits 65, their saliva and pancreatic secretions, both of which are involved in enzyme activity—can have declined by as much as 50%! This decline creates chronic indigestion, setting the stage for gut issues, yeast and mold overgrowth, even malnutrition. This is why I’m a big fan of enzyme and probiotic supplementation and one of the best companies I’ve ever found that specializes in optimizing your digestion through both of these supplements are my friends at BiOptimizers.Head on over to www.bioptimizers.com/boomer and use coupon code BOOMER to get 10% off any package. They have the best guarantee I’ve seen in the industry. It’s a 365 day FULL money back guarantee. If you want to try MassZymes, I strongly suggest you head on over to their site and grab it your free bottle before they either run out or just take down this offer. Head on over to https://masszymes.com/boomerfree and you’ll automatically get your free bottle added to your shopping cart.Disclaimer This information is being provided to you for educational and informational purposes only. This is being provided as a self-help tool to help you understand your genetics, biodata and other information to enhance your performance. It is not medical or psychological advice. Virtuosity LLC, or Decoding Superhuman, is not a doctor. Virtuosity LLC is not treating, preventing, healing, or diagnosing disease. This information is to be used at your own risk based on your own judgment. For the full Disclaimer, please go to (Decodingsuperhuman.com/disclaimer). See acast.com/privacy for privacy and opt-out information.

Utilizing Healthy Carbohydrates in Our Diet & Debunking the Carbs Are Bad Myth

The Primal Pioneer

Play Episode Listen Later Aug 3, 2020 75:24

In episode 24 of the Primal Pioneer, we are diving into why you should dissolve these limiting beliefs and how you don't have to take on a deprivation attitude when it comes to these foods. Instead, you can have carbs and sugars within your diet without pathological impacts on your body. Some topics we touch on include:⁣ How a light environment plays a crucial role in how we process and digest carbohydrates.⁣ When your food is turned into energy, it's not detected just as fats, proteins, and carbohydrates. The food is also broken down into a more anatomical level involving protons and electrons. ⁣ We look to diet to rectify metabolic disorders, however, diet is a band-aid approach to rectifying these issues.⁣ Cytochrome 1 (NAD NADH) needs UV light to function optimally.⁣ ⁣ If you're someone who struggles with cravings of carbohydrates and sugars, or tries to stray away from these types of foods, I'm certain that after you tune in to episode 24, you will have the knowledge on how you can enjoy a healthy diet that still involves carbs and sugars. Be sure to tune in to episode 24 to learn more about how you can utilize health carbohydrates in your diet.⁣ ⁣ If you have enjoyed this episode of the podcast, take a screenshot, share it in your Instagram stories and tag me, @sunlight_rx.⁣ ⁣ CONNECT WITH HEATHAR:⁣ Website⁣ The Sunlight Rx EBook⁣ Instagram⁣ Facebook⁣ ⁣ WORK WITH HEATHAR:⁣ For additional guidance utilizing the healing powers of sunlight to improve nutrient and hormonal health and production, check out my Sunlight Rx Ebook at my website, heatharshepard.com!

YouTube Is Misleading You. Help Us Make It Better.

MinuteEarth

Play Episode Listen Later Jun 18, 2020 3:57

Join us on Patreon at http://patreon.com/MinuteEarth As we see a rise in misinformation on YouTube, educational channels like MinuteEarth need your support today more than ever. Thanks also to our YouTube members. ___________________________________________ To learn more, start your googling with these keywords: Misinformation: false information that is spread, regardless of intent to mislead Disinformation: deliberately misleading or biased information; manipulated narrative or facts ___________________________________________ Subscribe to MinuteEarth on YouTube: http://goo.gl/EpIDGd Support us on Patreon: https://goo.gl/ZVgLQZ And visit our website: https://www.minuteearth.com/ Say hello on Facebook: http://goo.gl/FpAvo6 And Twitter: http://goo.gl/Y1aWVC And download our videos on itunes: https://goo.gl/sfwS6n ___________________________________________ Credits (and Twitter handles): Video Writer, Director, and Narrator: Julián Gustavo Gómez (@thejuliangomez) Video Illustrator: Arcadi Garcia Rius (@garirius) With Contributions From: Henry Reich, Alex Reich, Kate Yoshida, Ever Salazar, Peter Reich, David Goldenberg, Sarah Berman Music by: Nathaniel Schroeder: http://www.soundcloud.com/drschroeder Image Credits: Emperor penguin photo by Cristopher Michel https://flic.kr/p/pKneEA Macaroni penguin photo by Liam Quinn https://flic.kr/p/9YG3s2 COX-2 graphics by Cytochrome c https://commons.wikimedia.org/wiki/File:Cyclooxygenase-2.png ___________________________________________ References: Anderson, Janna, and Lee Rainie. "The future of truth and misinformation online." Pew Research Center 19 (2017). “Why Is YouTube Broadcasting Climate Misinformation to Millions?” Avaaz, 16 Jan. 2020, http://secure.avaaz.org/campaign/en/youtube_climate_misinformation/. Del Vicario, Michela, et al. "The spreading of misinformation online." Proceedings of the National Academy of Sciences 113.3 (2016): 554-559.Iammarino, Nicholas K., and Thomas W. O’Rourke. "The challenge of alternative facts and the rise of misinformation in the digital age: Responsibilities and opportunities for health promotion and education." American journal of health education 49.4 (2018): 201-205. Lewis, Paul. "Fiction is outperforming reality”: How YouTube’s algorithm distorts truth." The Guardian 2 (2018): 2018. Meserole, Chris. "How misinformation spreads on social media—And what to do about it." The Brookings Institution (May 9, 2018), https://www.brookings. edu/blog/order-from-chaos/2018/05/09/how-misinformation-spreads-on-social-media-and-what-to-do-about-it (2018). O'Connor, Cailin. How Misinformation Spreads-and Why We Trust It. Scientific American, Sept. 2019, http://www.scientificamerican.com/article/how-misinformation-spreads-and-why-we-trust-it/. Roberts, David. YouTube Has a Big Climate Misinformation Problem It Can't Solve. Vox, 26 Jan. 2020, http://www.vox.com/energy-and-environment/2020/1/26/21068473/youtube-climate-change-misinformation-epistemic-crisis. Syed-Abdul, Shabbir, et al. "Misleading health-related information promoted through video-based social media: anorexia on YouTube." Journal of medical Internet research 15.2 (2013): e30.Williamson, Phil. "Take the time and effort to correct misinformation." Nature 540.7632 (2016): 171-171. Wood, Mike. “How Does Misinformation Spread Online?” Psychology Today, Sussex Publishers, 6 Dec. 2018, http://www.psychologytoday.com/us/blog/web-mistrust/201812/how-does-misinformation-spread-online. Educational creators featured in this video: Jordan Harrod – https://www.youtube.com/channel/UC1H1NWNTG2Xi3pt85ykVSHA SciShow – https://www.youtube.com/user/scishow Tom Scott – https://www.youtube.com/user/enyay ASAP Science – https://www.youtube.com/user/AsapSCIENCE ViHart – https://www.youtube.com/user/Vihart DrawCuriosity – https://www.youtube.com/channel/UCOs_jEnQF2ePJzjJTgRtunA TierZoo – https://www.youtube.com/channel/UCHsRtomD4twRf5WVHHk-cMw Wannabe Linguist – https://www.youtube.com/channel/UCkl3U62tqz-4SDxbqjn4G7A Kurzgesagt – https://www.youtube.com/user/Kurzgesagt Sabrina Cruz – https://www.youtube.com/user/NerdyAndQuirky msbeautyphile – https://www.youtube.com/user/msbeautyphile CGP Grey – https://www.youtube.com/user/CGPGrey Hot Mess – https://www.youtube.com/channel/UCsaEBhRsI6tmmz12fkSEYdw Jabrils – https://www.youtube.com/channel/UCQALLeQPoZdZC4JNUboVEUg CrashCourse – https://www.youtube.com/user/crashcourse Tippe Top Physics – https://www.youtube.com/user/tippetopphysics

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Guidance Recap Podcast | In Vitro Drug Interaction Studies — Cytochrome P450 Enzyme- and Transporter-Mediated Drug Interactions Final Guidance

FDA Guidance Recap Podcast

Play Episode Listen Later Feb 28, 2020 14:05

Guidance Recap Podcast | In Vitro Drug Interaction Studies — Cytochrome P450 Enzyme- and Transporter-Mediated Drug Interactions Final Guidance - Podcast Transcript

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Guidance Recap Podcast | Clinical Drug Interaction Studies — Cytochrome P450 Enzyme- and Transporter-Mediated Drug Interactions Final Guidance

FDA Guidance Recap Podcast

Play Episode Listen Later Feb 28, 2020 6:54

Clinical Drug Interaction Studies — Cytochrome P450 Enzyme- and Transporter-Mediated Drug Interactions Final Guidance - Podcast Transcript

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(HumanCare podcast) How to Advocate for Yourself: Em and Kate Miller

Invisible Not Broken A Chronic Illness Podcast

Play Episode Listen Later Jan 29, 2020 69:00

“You know your body better than anyone. You’re living in it 24/7. No one should be dismissing the stuff you have to say.”-Em MillerEm and Kate Miller are the co-authors of chronic illness blog, TwoBeingHealthy.com and the YouTube channel of the same name. Forced into non-traditional careers by chronic illnesses that include Lupus, POTS, EDS, Mast Cell Activation disorder diagnosed in their late teens, their blog is a delightful mix of practical tips for patients, product testing, and their own struggles. Today they share their journey, tips on how to advocate for yourself as a patient, and the importance of community support.Visit:Blog: https://www.twobeinghealthy.com/YouTube channel: http://bit.ly/2TOvA7EDoctors Appointment – Our Top 10 Tips! : http://bit.ly/2sO6DxXInstagram: @twobeinghealthyTime Stamps:17:58 – Em’s diagnosis of Lupus at 1718:55 – Kate’s diagnosis and that people typically have more than one autoimmune disorder19:20 – POTS diagnosis19:28 – What is POTS20:20 – Difference between how Em and Kate experience their illnesses22:16 – What is EDS23:24 – Perceptions of chronic illness and breaking the stigma28:00 – Empowering aspect of the TwoBeingHealthy blog29:04 – Examples of what they share on their blog30:50 – Problem with doctors assuming patients with the same conditions will have the same traits31:30 – The importance of advocating for yourself at doctor’s appointments32:39 – The importance of not wearing makeup or nailpolish to doctors’ appointments 37:22 – The importance of tracking your symptoms and having notes of everything you want to cover during the appointment38:55- Knowing the tests to ask for re EDS and POTS + the problem with POTS43:13 – How to act with a new doctor and a time constraint44:04 – What to do if you feel you’re not being taken seriously by the doctor46:16 – The importance of finding a doctor you can trust49:20 – Problems communicating with doctors, especially renowned specialists52:32 – Cytochrome mutations and their effect on medication absorption53:54 – Difference between advocating for oneself and making demands55:54 – Importance of mutual respect in doctor patient relationships and finding a doctor you trust59:45 – On Em and Kate’s unsponsored product testing1:01:37 – The importance of personal comfort1:04:10 – The importance of finding what works for you 1:04:49 – Benefits of having an emergency relief kit1:06:47 – The Chronic Babe and being as well as possible1:07:27 – The big impact of little changes and recommendations1:08:10 – The importance of health and being proactive1:09:10 – What is Mast Cell Activation Disorder1:14:11 – The chronic illness community that developed around the blog1:17:45 – The challenge of balancing the difficult and raw with the positive and proactive1:19:50 – The benefit of having someone vs going it alone1:20:38 – The upside of following other people’s chronic illness journeys on social media1:21:52 – Importance of community, partnerships, and trust SHARE

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Red Light Magic for Biohacking Cell Repair

Root2Crown Podcast

Play Episode Listen Later Apr 29, 2019 94:29

We are solar powered beings! But we now spend 93% of our lives INDOORS. Brilliant founder of Sauna Space, Brian Richards, takes us through the fascinating body-wide healing phenomena of red light therapy. We cover all the science, the applications, and the specifics of how biologically relevant light (found largely in firelight, sunrise, and sunset) can cause massive changes in cell behavior, function, and repair. There are hundreds of research studies on this subject. Over 400 gold-standard, placebo-controlled clinical trials exist on this subject. It's only a matter of time before we see tanning salons and 7-Elevens popping up with this sort of therapy. Learn the facts now and become a savvy consumer on the good stuff. Our bodies are solar panels that need to be fueled by the light that nourishes them. If after this episode, you feel compelled to order a SaunaSpace product of your own, you can use promo code "AMRONMD" to receive a discount on your order.

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Episode 6: Cytochrome C - 16.10.2018

Les protéines se mettent à table - RTS

Play Episode Listen Later Oct 16, 2018 15:59

cytochrome

IBP053 - Diane Cytochrome [www.intransikbeats.com]

Intransikbeats Records

Play Episode Listen Later Sep 8, 2018 57:42

Welcome to our 53rd Episode of the IntransikBeats Podcast, to prepare for the transition of the autumn days smoothly, we're glad to present to you an hour of the finest selection of dynamic paced techno variety mixed by 'Diane Cytochrome' from Lyon, France. With a classical music background at the conservatory, Diane became very passionate about electronic music culture and gave up the piano and her cello for turntables. In her artistic approach, she forms her universe by drawing inspiration from different trends to forge her intimate vision of music. The desired aesthetic: find the light in the dark, vector of hope like life after death, a world where the vibrations are contrasted through heavy, powerful and melodic sounds. The Techno influence essentially consolidates this dark universe contrasted by the light. A singular universe without complacency through its sound selection without boundaries. Diane opened 'Les Nuits Sonores 2013' in Lyon, by mixing at the inauguration of the Festival. The 2013/2014 season marks her professionalization in the performing field as a DJ, with her residency 'CYTOCHROME' at the Terminal Club in Lyon. A lot has happened for her since then and a lot of promising projects in Europe are to be announced soon, so make sure to check her links out down below to support as usual ;) In the meantime, we hope you enjoy this podcast as much as we do and we ll catch you next month, thank you for the great support ! Tracklisting: DVM - Cultural difference Falhaber - That One Night 90 Process - Alter Ego dynArec - Criticize - dynarec remix X - H - X - Come for U NTBR - ISLAND JKS - Inside Out AIROD - Shockwave planners FUERR - Khörög Zurag ILLINURSE - Ein Zwei Polizei Basswell - Intense Euphoria NTBR - PLAYA DE AJO Brain 6 - Observer Swedish sisters UVB remix Klamer - Lonely persecuted soul TRBL - Voluctris (NTBR Edit) Fresh Sounds https://soundcloud.com/dianecytochrome Follow her activity @ https://www.facebook.com/dianecytochrome/?ref=hl More Mixes @ https://www.mixcloud.com/hopdiane/

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Cytochrome P450: Chemistry in its element

Chemistry in its element

Play Episode Listen Later Jun 3, 2014 5:23

Nathan Adams investigates some of the most important molecular machines within our cells, the cytochrome p450 enzymes

chemistry element nathan adams p450 cytochrome

Cytochrome C 6A

Fakultät für Biologie - Digitale Hochschulschriften der LMU - Teil 04/06

Play Episode Listen Later Dec 2, 2011

Fri, 2 Dec 2011 12:00:00 +0100 https://edoc.ub.uni-muenchen.de/14644/ https://edoc.ub.uni-muenchen.de/14644/1/Scharfenberg_Michael.pdf Scharfenberg, Michael ddc:570, ddc:500, Fakultät für Biologie 0

biologie fakult cytochrome ddc:500 scharfenberg ddc:570

Different mutation patterns of atovaquone resistance to Plasmodium falciparum in vitro and in vivo: rapid detection of codon 268 polymorphisms in the cytochrome b as potential in vivo resistance marker

Medizin - Open Access LMU - Teil 13/22

Play Episode Listen Later Jan 1, 2003

Background: Resistance of Plasmodium falciparum to atovaquone in vitro and in vivo has been associated to mutations in the parasite cytochrome b gene. Methods: Cultures were sequentially subjected to increasing doses of atovaquone alone or in combination with cycloguanil and the cytochrome b gene was sequenced. Additionally, we investigated the parasite cytochrome b gene of a patient returning from Mali with Malarone(R) treatment failure in vivo. Results: All strains that survived atovaquone concentrations in vitro of 2 x 10(-8) to 2 x 10(7) M showed the M1331 mutation and one strain with the highest atovaquone concentration the additional mutation L171F. Sequencing of the in vivo treatment failure revealed a point mutation at codon 268 resulting in an amino acid change from tyrosine to serine. Based on the repeated emergence of mutations at codon 268, but no detection of alterations at codon 133 in vivo, we developed a detection method for the diagnostic of codon 268 polymorphisms as a potential atovaquone/proguanil resistance marker. A nested PCR with 3 different pairs of primers for the second round was designed. Each product was digested with restriction enzymes, capable to distinguish the wild type from the two reported mutations at codon 268. Conclusion: Mutations at codon 268 of the parasite cytochrome bc(1) gene are associated with atovaquone/proguanil treatment failure in vivo and can be used as potential resistance marker This method provides a novel and robust tool to investigate the relevance of codon 268 polymorphisms as resistance marker and to monitor the further emergence of atovaquone/proguanil resistance.

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Targeting of cytochrome b2 into the mitochondrial intermembrane space

Medizin - Open Access LMU - Teil 10/22

Play Episode Listen Later Jun 1, 1993

Cytochrome b2 contains 2-fold targeting information: an amino-terminal signal for targeting to the mitochondrial matrix, followed by a second cleavable sorting signal that functions in directing the precursor into the mitochondrial intermembrane space. The role of the second sorting sequence was analyzed by replacing one, two or all of the three positively charged amino acid residues which are present at the amino-terminal side of the hydrophobic core by uncharged residues or an acidic residue. With a number of these mutant precursor proteins, processing to the mature form was reduced or completely abolished and at the same time targeting to the matrix space occurred. The accumulation in the matrix depended on a high level of intramitochondrial ATP. At low levels of matrix ATP, the mutant proteins were sorted into the intermembrane space like the wild-type precursors. The results: (i) suggest the existence of one or more matrix components that specifically recognize the second sorting signal and thereby trigger the translocation into the intermembrane space; (ii) indicate that the mutant signals have reduced ability to interact with the recognition component(s) and then embark on the default pathway into the matrix by interacting with mitochondrial hsp70 in conjunction with matrix ATP; (iii) strongly argue against a mechanism by which the hydrophobic segment of the sorting sequence stops translocation in the hydrophobic phase of the inner membrane.

space targeting medizin atp mitochondrial cytochrome

Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space

Medizin - Open Access LMU - Teil 09/22

Play Episode Listen Later Mar 20, 1992

Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export. The bacterial-type export sequence in pre-cytochrome b2 functions by inhibiting the ATP-dependent release of the protein from hsp60. Release for export apparently requires, in addition to ATP, the interaction of the signal sequence with a component of the export machinery in the inner membrane. Export can occur before import is complete provided that a critical length of the polypeptide chain has been translocated into the matrix. Thus, hsp60 combines two activities: catalysis of folding of proteins destined for the matrix, and maintaining proteins in an unfolded state to facilitate their channeling between the machineries for import and export across the inner membrane. Antifolding signals such as the hydrophobic export sequence in cytochrome b2 may act as switches between these two activities.

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Import of cytochrome c heme lyase into mitochondria

Medizin - Open Access LMU - Teil 09/22

Play Episode Listen Later Feb 1, 1992

Cytochrome c heme lyase (CCHL) catalyses the covalent attachment of the heme group to apocytochrome c during its import into mitochondria. The enzyme is membrane-associated and is located within the intermembrane space. The precursor of CCHL synthesized in vitro was efficiently translocated into isolated mitochondria from Neurospora crassa. The imported CCHL, like the native protein, was correctly localized to the intermembrane space, where it was membrane-bound. As with the majority of mitochondrial precursor proteins, CCHL uses the MOM19-GIP receptor complex in the outer membrane for import. In contrast to proteins taking the general import route, CCHL was imported independently of both ATP-hydrolysis and an electrochemical potential as external energy sources. CCHL which lacks a cleavable signal sequence apparently does not traverse the inner membrane to reach the intermembrane space; rather, it translocates through the outer membrane only. Thus, CCHL represents an example of a novel, 'non-conservative' import pathway into the intermembrane space, thereby also showing that the import apparatus in the outer membrane acts separately from the import machinery in the inner membrane.

import medizin atp mitochondria heme cytochrome cchl neurospora

Puzzling subunits of mitochondrial cytochrome reductase

Medizin - Open Access LMU - Teil 08/22

Play Episode Listen Later May 1, 1990

The ubiquinol-cytochrome c reductase complex, like the other proton-pumping respiratory complexes of mitochondria, is an assembly of many different subunits. However, only a few of these subunits participate directly in the electron transfer and proton translocation. The roles of the other subunits are largely unknown. We discuss here some intriguing features of two of these subunits.

medizin puzzling mitochondrial cytochrome reductase

Biogenesis of cytochrome c1

Play Episode Listen Later Jun 15, 1989

The biogenesis of cytochrome c1 involves a number of steps including: synthesis as a precursor with a bipartite signal sequence, transfer across the outer and inner mitochondrial membranes, removal of the first part of the presequence in the matrix, reexport to the outer surface of the inner membrane, covalent addition of heme, and removal of the remainder of the presequence. In this report we have focused on the steps of heme addition, catalyzed by cytochrome c1 heme lyase, and of proteolytic processing during cytochrome c1 import into mitochondria. Following translocation from the matrix side to the intermembrane-space side of the inner membrane, apocytochrome c1 forms a complex with cytochrome c1 heme lyase, and then holocytochrome c1 formation occurs. Holocytochrome c1 formation can also be observed in detergent-solubilized preparations of mitochondria, but only after apocytochrome c1 has first interacted with cytochrome c1 heme lyase to produce this complex. Heme linkage takes place on the intermembrane- space side of the inner mitochondrial membrane and is dependent on NADH plus a cytosolic cofactor that can be replaced by flavin nucleotides. NADH and FMN appear to be necessary for reduction of heme prior to its linkage to apocytochrome c1. The second proteolytic processing of cytochrome c1 does not take place unless the covalent linkage of heme to apocytochrome c1 precedes it. On the other hand, the cytochrome c1 heme lyase reaction itself does not require that processing of the cytochrome c1 precursor to intermediate size cytochrome c1 takes place first. In conclusion, cytochrome c1 heme lyase catalyzes an essential step in the import pathway of cytochrome c1, but it is not involved in the transmembrane movement of the precursor polypeptide. This is in contrast to the case for cytochrome c in which heme addition is coupled to its transport directly across the outer membrane into the intermembrane space.

medizin heme biogenesis nadh cytochrome fmn

Import of cytochrome c into mitochondria

Play Episode Listen Later Jan 1, 1989

The covalent attachment of heme to apocytochrome c, and therefore the import of cytochrome c into mitochondria, is dependent on both NADH plus a cytosolic cofactor that has been identified to be FMN or FAD. NADH in concert with flavin nucleotides mediates the reduction of heme. Heme in the reduced state is a prerequisite for its covalent attachment to apocytochrome c by the enzyme cytochrome c heme lyase and thus for subsequent translocation of cytochrome c across the outer mitochondrial membrane during import.

import medizin mitochondria fad heme nadh cytochrome fmn

Role of cytochrome c heme lyase in the import of cytochrome c into mitochondria

Play Episode Listen Later Dec 15, 1988

The import of cytochrome c into Neurospora crassa mitochondria was examined at distinct stages in vitro. The precursor protein, apocytochrome c, binds to mitochondria with high affinity and specificity but is not transported completely across the outer membrane in the absence of conversion to holocytochrome c. The bound apocytochrome c is accessible to externally added proteases but at the same time penetrates far enough through the outer membrane to interact with cytochrome c heme lyase. Formation of a complex in which apocytochrome c and cytochrome c heme lyase participate represents the rate-limiting step of cytochrome c import. Conversion from the bound state to holocytochrome c, on the other hand, occurs 10-30-fold faster. Association of apocytochrome c with cytochrome c heme lyase also takes place after solubilizing mitochondria with detergent. We conclude that the bound apocytochrome c, spanning the outer membrane, forms a complex with cytochrome c heme lyase from which it can react further to be converted to holocytochrome c and be translocated completely into the intermembrane space.

conversion formation import medizin mitochondria heme cytochrome neurospora

A mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria

Medizin - Open Access LMU - Teil 06/22

Play Episode Listen Later Jul 5, 1988

The nuclear cyt-2-1 mutant of Neurospora crassa is characterized by a gross deficiency of cytochrome c (Bertrand, H., and Collins, R. A. (1978) Mol. Gen. Genet. 166, 1-13). The mutant produces mRNA that can be translated into apocytochrome c in vitro. Apocytochrome c is also synthesized in vivo in cyt-2-1, but it is rapidly degraded and thus does not accumulate in the cytosol. Mitochondria from wild-type cells bind apocytochrome c made in vitro from either wild-type or cyt-2-1 mRNA and convert it to holocytochrome c. This conversion depends on the addition of heme by cytochrome c heme lyase and is coupled to translocation of cytochrome c into the intermembrane space. Mitochondria from the cyt-2-1 strain are deficient in the ability to bind apocytochrome c. They are also completely devoid of cytochrome c heme lyase activity. These defects explain the inability of the cyt-2-1 mutant to convert apocytochrome c to the holo form and to import it into mitochondria.

activity import medizin mrna mutant bertrand mitochondria mol deficient heme genet cytochrome neurospora apocytochrome

Deficiency in mRNA splicing in a cytochrome c mutant of neurospora crassa

Play Episode Listen Later Jul 1, 1987

Molecular cloning and characterization of cytochrome c cDNA clones of Neurospora crassa wild-type (74A) and a cytochrome c-deficient mutant (cyc1-1) are described. Southern blot analysis of genomic DNA indicates that only one cytochrome c gene exists in the N. crassa genome. The cDNA sequence of the wild-type cytochrome c confirmed the previously determined protein sequence. Sequence analysis of the cyc1-1 cDNA for cytochrome c revealed the presence of a larger open reading frame, owing to the presence of an unspliced intron in the 3' end of the coding region. Splicing of this intron is obviously prevented due to the presence of two base exchanges in the highly conserved intron consensus sequences. Consequently, cyc1-1 synthesizes apocytochrome c with an altered carboxy terminus, 19 amino acids longer than the wild-type cytochrome c, with the final 27 amino acids being of an unrelated sequence. This alteration in the carboxy terminus renders the apocytochrome c incompetent for binding to mitochondria and, consequently, import into mitochondria. Thus, unlike other mitochondrial precursor proteins, where it has been demonstrated that the amino terminus alone is sufficient to target the protein to the mitochondria, an intact carboxy terminus is required for efficient import of apocytochrome c into mitochondria. This is independent confirmation for the view that the import pathway of cytochrome c is unique with respect to all other mitochondrial proteins studied to date.

dna southern medizin mrna mutant sequence molecular deficiency splicing cdna cytochrome neurospora

Import of cytochrome c into mitochondria

Medizin - Open Access LMU - Teil 06/22

Play Episode Listen Later Apr 1, 1987

The import of cytochrome c into mitochondria can be resolved into a number of discrete steps. Here we report on the covalent attachment of heme to apocytochrome c by the enzyme cytochrome c heme lyase in mitochondria from Neurospora crassa. A new method was developed to measure directly the linkage of heme to apocytochrome c. This method is independent of conformational changes in the protein accompanying heme attachment. Tryptic peptides of [35S]cysteine-labelled apocytochrome c, and of enzymatically formed holocytochrome c, were resolved by reverse-phase HPLC. The cysteine-containing peptide to which heme was attached eluted later than the corresponding peptide from apocytochrome c and could be quantified by counting 35S radioactivity as a measure of holocytochrome c formation. Using this procedure, the covalent attachment of heme to apocytochrome c, which is dependent on the enzyme cytochrome c heme lyase, could be measured. Activity required heme (as hemin) and could be reversibly inhibited by the analogue deuterohemin. Holocytochrome c formation was stimulated 5–10-fold by NADH > NADPH > glutathione and was independent of a potential across the inner mitochondrial membrane. NADH was not required for the binding of apocytochrome c to mitochondria and was not involved in the reduction of the cysteine thiols prior to heme attachment. Holocytochrome c formation was also dependent on a cytosolic factor that was necessary for the heme attaching step of cytochrome c import. The factor was a heat-stable, protease-insensitive, low-molecular-mass component of unknown function. Cytochrome c heme lyase appeared to be a soluble protein located in the mitochondrial intermembrane space and was distinct from the previously identified apocytochrome c binding protein having a similar location. A model is presented in which the covalent attachment of heme by cytochrome c heme lyase also plays an essential role in the import pathway of cytochrome c.

activity import medizin mitochondria nadh hplc nadph cytochrome neurospora 35s

Enzymatic formation of protopines by a microsomal cytochrome P-450 system of Corydalis vaginans

Chemie und Pharmazie - Open Access LMU - Teil 01/02

Play Episode Listen Later Jan 1, 1987

A microsomal cytochrome P-450-NADPH dependent enzyme which hydroxylates stereo- and regiospecifically carbon atom 14 of (S)- -N- methyltetrahydroprotoberberines has been discovered in a number of plant cell cultures originating from species containing protopine alkaloids; the monooxygenase was solubilized, partially purified (100-fold) and characterized.

system formation sn nadph enzymatic cytochrome chemie und pharmazie

Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

Medizin - Open Access LMU - Teil 05/22

Play Episode Listen Later Jan 1, 1986

The Fe/S protein of complex III is encoded by a nuclear gene, synthesized in the cytoplasm as a precursor with a 32 residue amino-terminal extension, and transported to the outer surface of the inner mitochondrial membrane. Our data suggest the following transport pathway. First, the precursor is translocated via translocation contact sites into the matrix. There, cleavage to an intermediate containing an eight residue extension occurs. The intermediate is then redirected across the inner membrane, processed to the mature subunit, and assembled into complex III. We suggest that the folding and membrane-translocation pathway in the endosymbiotic ancestor of mitochondria has been conserved during evolution of eukaryotic cells; transfer of the gene for Fe/S protein to the nucleus has led to addition of the presequence, which routes the precursor back to its “ancestral” assembly pathway.

protein transport medizin sorting mitochondria fes ubiquinol cytochrome reductase

Transport of cytochrome c heme lyase

transport medizin bernd helmut hennig heme cytochrome

Play Episode Listen Later Jan 1, 1983

Sat, 1 Jan 1983 12:00:00 +0100 https://epub.ub.uni-muenchen.de/7423/1/7423.pdf Neupert, Walter; Köhler, Helmut; Hennig, Bernd ddc:610, Medizin

Biogenesis of cytochrome c in Neurospora crassa

Play Episode Listen Later Jan 1, 1983

Sat, 1 Jan 1983 12:00:00 +0100 https://epub.ub.uni-muenchen.de/7398/1/7398.pdf Neupert, Walter; Hennig, Bernd ddc:610, Medizin

medizin bernd hennig biogenesis cytochrome neurospora

Structural role of the tyrosine residues of cytochrome c

Play Episode Listen Later Jul 1, 1982

The tertiary structures of horse, tuna, Neurospora crassa, horse [Hse65,Leu67]- and horse [Hse65,Leu74]-cytochromes c were studied with high-resolution 1H n.m.r. spectroscopy. The amino acid sequences of these proteins differ at position 46, which is occupied by phenylalanine in the horse proteins but by tyrosine in the remaining two, and at positions 67, 74 and 97, which are all occupied by tyrosine residues in horse and tuna cytochrome c but in the other proteins are substituted by phenylalanine or leucine, though there is only one such substitution per protein. The various aromatic-amino-acid substitutions do not seriously affect the protein structure.

medizin structural tyrosine residues cytochrome neurospora

H NMR Studies of Eukaryotic Cytochrome c