It’s possible that I shall make an ass of myself. But in that case one can always get out of it with a little dialectic. I have, of course, so worded my proposition as to be right either way (K.Marx, Letter to F.Engels on the Indian Mutiny)
Friday, October 09, 2026
The story behind the butterfly’s enhanced visual world of color
Researchers discovered the genetic switch that produces extra light-detecting cells that led to the ability to recognize more colors in flowers and other butterflies
Many insects see the world through hundreds of tiny lenses that are grouped together in a visual organ known as the compound eye. Behind each lens sits a cluster of eight light-detecting cells arranged in a pattern that scientists believe has existed for hundreds of millions of years.
Butterflies are the rare exception. They are equipped with nine light-detecting cells, which gives them the ability to visually navigate a much richer world of color, compared with insects such as flies, and allows them to locate nectar and potential mates.
University of California San Diego scientists in School of Biological Sciences Associate Professor Michael Perry’s lab have discovered the genetic modification that gave butterflies this visual advantage.
“Butterflies see far more color than flies do because at some point in their evolution they added a photoreceptor to every unit of their compound eye — a rare break from an eye design that has otherwise been conserved across insects for hundreds of millions of years,” said Perry, a faculty member in the Department of Cell and Developmental Biology. “We found the genetic switch that did it.”. “We found the genetic switch that did it.”
In a study published in the journal Science Advances, Perry and his coauthors identified the genetic steps involved in the emergence of the ninth photoreceptor in painted lady butterflies, the most widespread butterfly species in the world. While flies feature light-sensing cells known as photoreceptors R1-R8, butterflies expanded their color vision by adding a second R7 photoreceptor to each unit of the eye, the researchers found. To test whether that genetic change was enough on its own, they recreated it in a fruit fly — switching on a gene in cells that normally keeps it off, and timing it to the brief window when the eye is being built. This produced a “butterfly fly” that grows its eyes on the butterfly plan, with nine cells per eye unit instead of eight.
A new light detector in the eye would be of no use if the brain is not able to connect to the new information provided by that detector. The scientists assumed that adding a sensory input such as a new photoreceptor unit should require the brain to slowly evolve a matching neuron partner that would receive information on the other end. That didn’t happen, the researchers found. To their surprise, no adaptive change was needed.
The fly brain regularly overproduces neurons that die off if they fail to find a connection. The brain of the butterfly-fly, they found, knew precisely how to handle the new photoreceptor by using its extra “standby” neurons and put them in play.
“When we gave those spare neurons something to connect to, they survived and wired up correctly — immediately — with no further genetic change,” said Perry. “In other words, the brain was ready before the eye asked. This is a rare, concrete case of evolution making use of neurons that were otherwise going to die.”
The new study’s findings provide a glimpse of how insects, with a flexible brain framework, were able to accommodate new inputs to evolutionarily adapt to an emerging need in their environment: an elevated ability to visualize flowering plants.
The team also found a hawkmoth that appears to be partway through the same transition: the lower half of its eye is butterfly-like, with two of these cells per unit, while the upper half is fly-like, with one. That is roughly what you would expect if the change began in one region of the eye and spread.
The research team is now exploring further unanswered questions, such as the difficult-to-study issue of whether the butterfly-fly can in fact see more vivid color with the additional photoreceptor, as butterflies do.
Flowers become harder to smell for bees, moths and other pollinating insects in polluted air, according to research led by the University of Reading.
Scientists analysed 22 experimental studies on how the air pollutants ozone and nitrogen oxides (NOx) affect pollinators. Both pollutants make it harder for pollinators to find flowers by breaking down or altering the scents that flowers give off.
The new research, published in the journal Frontiers in Ecology and the Environment, found that elevated ozone reduced pollinator performance by an average of 42%, while NOx cut performance by 46%. When the two pollutants occurred together, the average reduction was 68%. Only a few studies tested both pollutants together, and in those the extra harm from combining them was smaller than the averages suggest. This is because the two gases react with each other in the air and partly cancel each other out.
Diesel vehicles produce most NOx pollution and can stay on roads for more than 20 years after the last new one is sold. The UK's delayed ban on new petrol and diesel cars, pushed from 2030 to 2035 risks extending the damage to pollinators.
Dr James Ryalls, lead author of the study at the University of Reading, said: “Ozone levels are projected to keep rising until around 2050, even as NOx emissions begin to fall as the world moves away from fossil fuels. This creates a difficult period for pollinators over the next two-to-three decades. Once cleaner fuels take over fully, ozone levels should decline, giving pollinators a chance to recover.
“How quickly that recovery happens depends on the choices governments make now. Cutting NOx emissions faster, especially from diesel vehicles, could shorten the difficult period and speed up recovery.
"Most of the food we grow depends on healthy pollinators, so protecting them from pollution cannot wait until 2050."
The study also found:
Specialist pollinators reliant on one plant's scent, such as some moths, are more at risk than generalists like many bees.
Day-active pollinators such as bees and butterflies face higher ozone levels, while night-active pollinators (including many moths) encounter higher nitrogen oxides. Both need protection.
Most evidence came from Europe, leaving a gap in understanding the risks to pollinators in more heavily polluted regions such as parts of Asia.
If you hate needles, music might make you feel better during a cannula insertion… but it has to be the right kind of music. Although different musical interventions have repeatedly been reported to help with pain and stress, the evidence varies widely for different types of music and it’s hard to figure out what works best. To investigate, scientists played different kinds of music for patients about to undergo an intravenous cannula before an MRI — either Mozart, relaxation music, or the patients’ own favorite tunes. They found that playing patients’ favorite music worked best.
“Although a needle puncture is a minor procedure, the level of pain can vary significantly from person to person,” said Dr Andrei Cristinel Dragnea of University Hospital Zürich, lead author of the article in Frontiers in Pain Research. “In modern medicine, the goal of treating physicians is not only to provide a successful diagnosis and therapy, but also to ensure that the procedure causes as little discomfort as possible.”
“I would recommend listening to music to patients, especially patients who like music in general,” said Dr Meritxell Garcia Alzamora of University Hospital Zürich, senior author of the article. “In view of our results we will increase the application of music in venous punctures performed for radiological procedures, especially in anxious or claustrophobic patients.”
Sweet music?
The scientists recruited 204 patients undergoing a non-emergency MRI of the brain, spine, or head and neck. These patients’ procedures called for a contrast agent inserted into their veins with a cannula, which can hurt. A quarter of them acted as a control group, meaning they listened to no music, while three other groups listened to either their favorite music, music specifically designed for relaxation, or a piece of Mozart, Sonata KV448, which several studies have found to have therapeutic properties.
Before the procedure started, patients assigned to the ‘favorite music’ group were asked to name an artist or song they would like to hear, and all patients were shown a visual scale that describes pain from a level of one (no pain) to 10 (worst pain of their life). This allowed the researchers to ask patients to rate their pain before and during the procedure, and then at two points afterwards — 30 seconds and two minutes later.
“From the four conditions we examined, only favorite music and Mozart showed a positive effect,” said Garcia Alzamora. “Favorite music manifested a significant pain reduction effect both in patients with and without baseline pain — i.e. with preexisting pain before needle puncture. Mozart only showed significant pain relief in patients with preexisting pain.”
Patients who were listening to their favorite music experienced less pain both 30 seconds and two minutes after the cannula was inserted. In a subgroup of patients who reported preexisting pain before cannulation, listening to their favorite music also reduced pain at the time of needle insertion, and listening to Mozart reduced pain two minutes after needle insertion.
Pain levels seemed to improve more two minutes after cannulation than at the earlier time points, although this data can’t explain why. It could be that the initial discomfort of the cannula pulled people’s attention from the music, or that the mechanisms which make music helpful for pain reduction need some time to kick in.
Relaxation music doesn’t soothe
However, Mozart only seemed to work for the patients who reported being in pain before the cannulation, and the patients who listened to relaxation music or no music didn’t experience any change in their pain.
“Relaxation music is usually characterized by a slow speed and low volume, and does not show noticeable dynamics,” said Garcia Alzamora. “These characteristics may have contributed to the patients disregarding relaxation music, which would explain the lack of pain relief.”
“The intervention — in this case the venous puncture — consisted only of a very short-term pain with a small needle, although this can be very painful for some patients,” cautioned Dragnea, adding that it would be worth evaluating the benefits of music for patients undergoing procedures that are more painful and last longer. “Additionally, a technician accompanying and talking to the patient could be regarded as a confounder, as the mere presence of a person talking to you may be perceived as calming and distracting. However, all patients were exposed to the same conditions, so this confounder should not be over-interpreted.”
Animated molecular movie of penicillin biosynthesis. Each frame shows a different stage of the reaction as IPNS converts its substrate into penicillin. The animation was reconstructed from several time-resolved X-ray crystal structures collected at different reaction times, allowing the complete catalytic process to be visualized at atomic resolution. Image credit: Patrick Rabe/University of Oxford and Greg Stewart/SLAC National Accelerator Laboratory.
Credit: Patrick Rabe/University of Oxford and Greg Stewart/SLAC National Accelerator Laboratory.
Researchers from the University of Oxford and international collaborators have revealed previously unseen rapid chemical stages in the formation of β-lactam antibiotics like penicillin, offering insights that can support future antibiotic development. The findings have been published today (9 Oct) in Nature Catalysis.
Ever since penicillin was developed into a working drug at the University of Oxford in the early 1940’s, β-lactam antibiotics have been among the most important medicines for treating bacterial infection. Their activity depends on a special ring - the β-lactam ring - a highly strained chemical ring system that interferes with bacterial cell wall synthesis, ultimately causing the cell wall to fail and the bacteria to die.
Scientists have been studying how nature constructs this β-lactam ring for decades, but the key fleeting reaction intermediates have been too difficult to observe directly.
Rising rates of antimicrobial resistance- a process in which bacteria, fungi and other microorganisms evolve to survive the medicines designed to kill them, are undermining the effectiveness of existing antibiotics. With too few new antibiotics in development, understanding how nature builds these molecules is an important step towards replenishing the antibiotic pipeline.
In the new study, researchers from the University of Oxford in collaboration with partners from Diamond Light Source, Lawrence Berkeley National Laboratory, PAL-XFEL and SLAC National Accelerator Laboratory have used X-ray free-electron lasers to observe the enzyme isopenicillin N synthase, or IPNS as it converts its linear peptide substrate into the ring system of penicillin.
The new study shows, in unprecedented detail, how the enzyme IPNS achieves an exceptionally complex transformation in a single step. This resolves a long-standing mechanistic question that has remained unanswered for more than four decades.
Rather than relying on static X-ray crystallographic structures of the enzyme, the researchers followed the reaction in real time using ultrafast X-ray free-electron laser (XFEL) experiments.
The team captured several rapid stages in the reaction. These included a thioaldehyde intermediate formed just before the β-lactam ring is created, and a monocyclic β-lactam intermediate, representing the first ring-shaped structure on the way to forming the complete penicillin scaffold. These steps provide the clearest picture yet of how the IPNS enzyme assembles the penicillin scaffold.
The work also showed that water molecules inside the enzyme play a key role in guiding the reaction. Subtle movements throughout the enzyme help guide these chemical steps, showing that both the enzyme's shape and its chemistry work together to control penicillin formation.
To capture the reaction in real time, the researchers used a system in which thousands of tiny droplets containing anaerobic enzyme microcrystals were deposited onto a moving 2 mm wide tape. As the tape entered an oxygen filled chamber, oxygen rapidly diffused into the crystals and initiated the reaction simultaneously across the sample. By precisely controlling the speed of the tape, the researchers could determine how long each crystal reacted before reaching the X-ray interaction point, where an ultrafast XFEL pulse recorded an atomic resolution snapshot.
Combining thousands of these snapshots allowed the team to build a frame-by-frame “molecular movie” of penicillin biosynthesis. This method allows individual reaction intermediates that exist only for tiny fractions of a second to be observed at atomic resolution, and under physiological temperature and pressure, before they disappear.
Oxford has played a central role in the history of penicillin since the pioneering work of Nobel prize-winning scientists Prof Howard Florey and Sir Ernst Chain, and colleagues, who developed penicillin into the first clinically useful antibiotic during the Second World War. This new study ultimately builds on the work of Nobel prize-winning Oxford chemist Dorothy Hodgkin, who first solved the structure of penicillin in 1945 using X-ray crystallography.
Beyond penicillin, IPNS belongs to a large family of iron-dependent oxygenase enzymes involved in human biology, including ones that enable us to sense and respond to changes in oxygen availability. The mechanistic insights from this work therefore have implications far beyond antibiotics, offering new principles for enzyme engineering and catalyst design.
Professor Christopher Schofield, Professor of Chemistry, University of Oxford, and a senior author of the paper, said, “Penicillin has shaped modern medicine, but there is still much to learn about how nature builds this important antibiotic structure. By capturing these fleeting steps, we can better understand how enzymes control complex chemistry with remarkable precision.
“As rates of antimicrobial resistance continue to rise, understanding this process will ultimately help us make existing antibiotics more efficient and design new antibiotic structures.”
Today, one in six bacterial infections is resistant to antibiotics. Rising resistance threatens decades of progress in cancer care, transplant surgery and other areas of modern medicine, while also placing pressure on economies, health systems and food production.
Dr Patrick Rabe, Wellcome Career Development Award Investigator, University of Oxford and first author on the paper said, “These insights matter because they can inform how we think about antibiotic biosynthesis and future strategies for developing antibacterial medicines. The ability to capture structural snapshots over milliseconds to seconds of reaction time allows us to connect enzyme motion, iron chemistry and water-mediated proton transfer. This gives us a much richer view of how IPNS controls a difficult chemical transformation. By understanding this process in atomic detail, we can begin to think about engineering these enzymes to produce new or improved antibiotic scaffolds.”
This study brought together expertise in structural biology, spectroscopy, chemistry, computation and enzyme engineering. This approach provides a powerful way to study fleeting chemical intermediates that have previously been inaccessible, both in antibiotic biosynthesis and in other biologically important enzyme reactions.
Dr Allen M Orville, group leader of the XFEL Hub and co-author of the paper, said: “The XFEL Hub at Diamond brought specialist expertise in time-resolved X-ray methods and XFEL-based structural biology to this study. Working closely with our colleagues in Oxford and at partner facilities, we helped bring together the experimental approaches needed to capture these fleeting stages of enzyme catalysis. The results show the power of combining complementary expertise and X-ray techniques to move beyond static structures and reveal how enzymes work in real time. It is a great example of how time-resolved structural biology can uncover new principles of enzyme function and, ultimately, inform the design of new catalysts and therapeutics.”
The study 'Unanticipated intermediates during isopenicillin N synthase catalysis identified by time-resolved X-ray free-electron laser studies' will be published in Nature Catalysis at 10 AM BST / 5 AM ET Friday 9 October 2026 at https://www.nature.com/articles/s41929-026-01618-4 To view a copy of the study before this under embargo, contact Avni Gupta avni.gupta@chem.ox.ac.uk.
The work was led by researchers in the Department of Chemistry, University of Oxford, in collaboration with Lawrence Berkeley National Laboratory, SLAC National Accelerator Laboratory and international partners.
Experiments were carried out using X-ray free-electron lasers at LCLS (USA), PAL-XFEL (Republic of Korea), SACLA (Japan) and Diamond Light Source (UK).
About the University of Oxford
Oxford University has been placed number 1 in the Times Higher Education World University Rankings for the tenth year running, and number 3 in the QS World Rankings 2024. At the heart of this success are the twin-pillars of our ground-breaking research and innovation and our distinctive educational offer.
Oxford is world-famous for research and teaching excellence and home to some of the most talented people from across the globe. Our work helps the lives of millions, solving real-world problems through a huge network of partnerships and collaborations. The breadth and interdisciplinary nature of our research alongside our personalised approach to teaching sparks imaginative and inventive insights and solutions.
Through its research commercialisation arm, Oxford University Innovation, Oxford is the highest university patent filer in the UK and is ranked first in the UK for university spinouts, having created more than 300 new companies since 1988. Over a third of these companies have been created in the past five years. The university is a catalyst for prosperity in Oxfordshire and the United Kingdom, contributing around £16.9 billion to the UK economy in 2021/22, and supports more than 90,400 full time jobs.
About Diamond Light Source
Diamond Light Source is the UK’s national synchrotron serving scientists and researchers from around the world. It is a not-for-profit joint venture funded by UK Research & Innovation (UKRI) and Wellcome. Diamond provides academic and industry researchers access to facilities that enable world-changing science. The machine generates extremely bright light that is directed into laboratories known as beamlines. Scientists use the light to find solutions to humanity’s most critical challenges, from health, food security and biotechnology to energy, climate change and advanced materials. Diamond is in the process of upgrading to a fourth-generation synchrotron, generating a brighter and more coherent light. This will provide enhanced imaging and analysis capabilities, helping the UK to remain at the forefront of scientific discovery.
Unanticipated intermediates during isopenicillin N synthase catalysis identified by time-resolved X-ray free-electron laser studies
Article Publication Date
9-Oct-2026
Short caption: Artistic concept of the ‘molecular movie’ method used to deduce how penicillin is made.
Extended caption: Molecular movie of penicillin biosynthesis. X-ray free electron laser experiments on isopenicillin N synthase microcrystals capture structural snapshots of key intermediates during the penicillin forming reaction. The film strip illustrates progression through the catalytic cycle, with the monocyclic β-lactam intermediate and reactive high valent ferryl iron species highlighted at the centre of the molecular movie.
Image credit: University of Oxford/Greg Stewart/SLAC National Accelerator Laboratory.
Creating a molecular movie of penicillin biosynthesis. Researchers used ultrafast X-ray free-electron laser pulses to capture atomic snapshots of an enzyme as it reacted with oxygen. Combining these snapshots produced a molecular movie showing how nature builds the core structure of penicillin.
Image credit: Greg Stewart/SLAC National Accelerator Laboratory
