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Portrait photograph of Professor Robert Huber.

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Alumni doing research

Professor Robert Huber

“I Went inside the Molecules”

13. Oct 2010 |

Reading time Min.

This interview is a republication of the original interview with Professor Huber from October 2010.

Professor Robert Huber, together with his colleague and former doctoral student Johann Deisenhofer and Harmut Michel, was awarded the Nobel Prize in Chemistry in 1988 for research into the three-dimensional structure of the reaction center of photosynthesis. The now 73-year-old scientist conducts research at the Max Planck Institute of Biochemistry in Martinsried near Munich when he is not teaching in Duisburg-Essen, Cardiff/ England, Barcelona or Seville/ Spain or at another international research institution.

Prof. Huber, you still feel connected to TUM.

Yes, I studied at the Technical University of Munich and literally absorbed science there. My first teachers, whom I had in the basic lectures and practical courses, all have big names in research. My mentor Walter Hoppe introduced me to crystallography. At the same time as me, Gerhard Ertl studied with his teacher Heinz Gerischer at the Institute of Physical Chemistry of the THM, in our time under the direction of the founder of the institute, Prof. Günther Scheibe. There we often ran into each other in the corridor of the old building on Luisenstraße. We were at the Scheibe Institute at the same time and both later won Nobel Prizes.

A good vintage then?

You could say that. We used very different approaches to research molecules. I worked on using crystallography to see inside the molecules to elucidate the structures. Ertl was interested in the surface structure. That’s quite nice, one was interested in the interior and the other in the surface. I went inside and then got my prize twenty years before him (laughs).

Picture: facesbyfrank/TUM.

Are you still at TUM?

Just yesterday I was in Garching with my former PhD student Prof. Michael Groll. I work with some younger researchers and am an associate professor at TUM. Until recently I also taught, but not anymore because the subject is very well represented by Groll. I am no longer needed there.

How do you feel about coming to TUM today?

Well, I studied at the main campus in Theresienstrasse. In this respect, I have more nostalgic feelings when I come to the city with the old buildings than when I go to Garching. In Garching, something would have to be done for the nostalgia, like creating more housing options, so that the campus is also busy on weekends. But the development is already fantastic! The catalysis center is currently under construction, a large building. I would like to praise President Herrmann and his perseverance.

You probably have a lot of former students.

I have had well over 100 PhD students in Germany alone and am surrounded by young scientists. Here in Munich, there are currently two: Prof. Michael Groll at TUM in biochemistry and Prof. Carl-Peter Hopfner at LMU. In Germany, about ten former students of mine have taken up academic careers, and others abroad.

Faraway islands and treasures buried there are probably no longer to be discovered, but countless protein molecules await the curious researcher who wants to understand the physics and chemistry of life. Curiosity and the desire for the adventure of research is something I experienced with my teachers at TUM.
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When did you start the research that led to the Nobel Prize?

Soon after my appointment at the Max Planck Institute of Biochemistry in Martinsried in 1972, we established the research group. The group consisted of chemists, physicists and biologists. The physicists worked more on the methodological problems, the biologists more on the biological aspects, and the chemists are generally very versatile and can do one and the other. Initially, there was a lot of need for methods and instruments. We developed our own machines. With appropriate methods and instruments, it was then possible to tackle the biological problems, to look at proteins that were biologically very interesting.

X-ray crystallography plays a crucial role in your research. What is it?

Crystallography is one of the tools we use to elucidate the structures of proteins. We can only understand life if we see the building blocks. Without seeing, there is certainly no understanding. Seeing does not yet mean understanding completely, but it is a basic requirement. Crystallography is used as a tool because it is a method that maps the atomic structure of these molecules, which are, after all, made up of many tens of thousands of atoms with a precisely defined structure. The protein must be imaged in its pure state, then it must be crystallized, exposed to X-rays, and the X-ray image interpreted. This is the task of X-ray crystallography.

What questions brought you to the Nobel Prize?

There was the question: How does photosynthesis work in a biological photocell? In technology, you use photocells in your camera. But how does it work in nature, in plants, in photosynthetic bacteria? To understand that, you have to isolate the components, crystallize them, and then elucidate the structure. That’s what we did. We not only solved the question of biological photosynthesis, but we faced the technical challenges. We showed that it is possible to analyze very large proteins. Further research then went in this direction: the elucidation of larger and more complex proteins. In the last ten years, a whole series of Nobel Prizes have been awarded for the analysis of large protein complexes.

They then also did research on autoimmune diseases.

That’s right. It turns out that many of the proteins we study have significance in medicine. By elucidating the structure of these molecules, we can, on the one hand, understand the cause of a disease and, on the other hand, possibly also influence the function of these molecules. Finally, we have elucidated a key molecule that plays a very crucial role in autoimmune diseases, but also a number of other molecules that are causative for diseases because they overfunction. If we know their structure, then we know how to influence function. For this kind of research, of course, we have a fantastic environment in Munich, with the two universities, the Max Planck Institutes and other research facilities. We can tell the chemists which molecules to synthesize according to the lock-and-key principle. We know the lock, can draw up a blueprint for the key, and the chemists build it. This has great significance for pharmaceutical research and pharmaceutical development.

Your research for pharmaceutical development is being implemented in two spin-offs. Is that a satisfying continuation of your work?

Definitely. In the first company, Proteros, which has now become very large, there are two aspects: One is that the company is applying the methods I developed in the early days of X-ray crystallography. The second aspect is the 70 jobs that have been created; quite a number of PhD students from the group have gotten interesting jobs as a result. With the second company, Suppremol, the satisfaction is also that an idea for a spin-off was born out of our basic academic research and the hope is to help patients with autoimmune diseases.

A private question at the end: Do you still ski?

I still go regularly because there is a traditional winter seminar in Klosters, Switzerland, which goes back to a colleague and friend at the Max Planck Institute for Biophysical Chemistry, Göttingen, Manfred Eigen. I joined this many years ago. So for the last 25 years or so, we have been getting our skis out regularly in January. We ski and exchange information about our research.

Robert Huber

Diploma Chemie 1960, Doctorate 1963, Habilitation 1968

Robert Huber passed his Abitur in 1956 at the Humanist Karlsgymnasium in Munich-Pasing. He then studied chemistry at the TUM and turned to crystallography and the structural elucidation of organic molecules in his diploma and doctoral theses under Walter Hoppe at the Max Planck Institute for Protein and Leather Research. He subsequently solved, in particular, the atomic structure of the insect pupal hormone ecdysone, which sparked his interest in biologically relevant macromolecules and the development of crystallographic techniques. In 1967, Huber set about the structural elucidation of the oxygen-binding insect protein erythrocruorin as part of his postdoctoral work with Hoppe, proving, among other things, the universality of globin folding.

In 1971, Robert Huber became director of the Department of Structural Research at the newly founded Max Planck Institute of Biochemistry in Martinsried near Munich. In 1976, he was appointed Professor of Chemistry at the TUM. He co-founded two biotech companies based in Martinsried that provide services for drug discovery and development in medicine (Proteros, 1997) and for the therapy of autoimmune diseases (Suppremol, 2005). Robert Huber has been an emeritus professor since 2005. In 2013, he was appointed by TUM President Wolfgang A. Herrmann into the circle of TUM Emeriti of Excellence.

Robert Huber received the Nobel Prize in Chemistry in 1988 together with his former PhD student TUM Alumnus Johann Deisenhofer and with Hartmut Michel for his major contributions to X-ray crystal structure analysis and elucidation of the spatial structure of the membrane reaction center of photosynthesis, the biological photocell.

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