Childhood & Early Life
Johann Deisenhofer was born on September 30, 1943 in Zusamaltheim, Bavaria, Germany to Thekla and Johann Deisenhofer. He has a younger sister, Antonie.
Upon returning from military service, senior Deisenhofer took to working at the family farm. He expected his son to tread on the same path but young Deisenhofer was interested in academics. He entered elementary school in 1949.
In 1956, he was sent to a series of boarding schools wherein he gained his higher education. Subsequently, he enrolled at the Augsburg's Holbein Gymnasium, graduating from the same in 1963.
Upon graduating, Deisenhofer attempted Germany’s qualifying examination. He secured a state scholarship that allowed him to attend the Technical University in Munich. However, to gain admission, he had to fulfill the requirement of a year and half of military service.
Following his military service, Deisenhofer began his studies at the University. Ever since a boy, he was fascinated by the astronomical problems and the physical world. As such, he dedicated his university study on the subject.
During his university education, he was drawn to the study of solid-state physics, the study of the composition and structure of condensed matter and solids. He was encouraged by his professors to explore and learn about the then upcoming genre of physics - biophysics - which was a study of biology using the principles of physical science.
He graduated with a diploma in physics from the University in 1971. The same year, his first ever scientific paper was published under the title, Physical Review Letters.
Continuing higher studies in the field of biophysics, he enrolled at the prestigious Max-Planck Institute for Biochemistry as a doctoral candidate. He studied under the direction of Institute’s director, Robert Huber.
While at the Max Planck institute, he dedicated his time to study of the technique of X-ray crystallography. He worked together with Wolfgang Steigemannon the crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor. In 1974, he submitted a thesis based on his work with Steigemann. The following year, the duo came up with a paper on their work titled ‘Acta Crystallographica’.
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Upon completing his PhD from Max Planck Institute, he took up the post of a postdoctoral fellow at the Institute offered to him by Huber. He worked as a research scientist alongside Huber, making advances in the applications for X-ray crystallography.
Apart from lab work, he designed computer programs that could process the data obtained from the X-ray techniques and produce a map of the atomic structure of the substance in question.
In 1976, Deisenhofer was appointed as a staff scientist at the Institute. Together with Peter M. Colman and Walter Palm, he started working on the human myeloma protein Kol. He collaborated with Huber to work on Peter Colman's work on the human Fc-fragment, and its complex with an Fc-binding fragment from protein A from Staphylococcus aureus. It was in 1980 that the refinement of these structures was finished.
Deisenhofer got involved in a variety of projects at Huber’s laboratory including human C3a, citrate synthase, and alpha-1 -proteinase inhibitor. Furthermore, he continued with his fascination for computers, developing and maintaining crystallographic software.
In 1979, German biophysicist Hartmut Michel joined Huber’s laboratory. Michel was engaged in the ongoing study of photosynthesis in the hopes of finding a way to obtain a thorough analysis of the molecules involved in the complex chemical-reaction process.
In 1981, Michel came up with a way to crystallize the photosynthetic reaction center of a purple bacterium, Rhodopseudomonasviridis. Next, Deisenhofer joined Michel in the latter’s study to determine the three-dimensional structure of the molecule. His experience in X-ray crystallography helped to analyze and map the photosynthetic reaction center.
With the help of several assistants, Deisenhofer was finally able to use X-ray crystallography techniques to map the more than 10,000 atoms within the membrane protein complex of Rhodopseudomonasviridis and produce the first three-dimensional structural analysis of a photosynthetic reaction center. It took him less than three years to come up with his findings.
Measuring the X-ray diffraction with the aid of electronic devices that had replaced the standard X-ray film was an easy task. However, the actual computer modelling process deemed out to be tough. It took Deisenhofer another two years to refine his research of the model of the membrane protein.
Using custom-designed software and a high-speed computer to quickly perform the myriad of calculations required to establish the location within the cell of each of the many thousands of atoms contained in that single crystallized protein, Deisenhofer meticulously supervised the slow formation of the model.
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The program devised by Deisenhofer, took the data relating to X-ray diffraction, combined it with the predetermined wavelength of the relevant radiation, and translated the resulting data into a three-dimensional computer model thus replacing the classic ball-and-stick models used by scientists until then.
The accomplishment gained by Michel, Deisenhofer and Huber created a storm in the scientific society as it was dubbed as the most important advancement in the understanding of photosynthesis since the mid-1960s. For their massive achievement, they were honored with the prestigious Nobel Prize.
Upon receiving the Nobel Prize, Deisenhofer came into limelight. He gained overnight stardom for his research work. Following his superlative success, he was asked to present papers and appeared at a host of science-related functions
In 1988, Deisenhofer moved to the United States, leaving his position at the Max Planck Institute. In the US, he accepted the Virginia and Edward Linthicum Distinguished Chair in Biomolecular Science at the University of Texas Southwestern Medical Center (UTSMC) at Dallas. He served as a Regental Professor
Other than serving as a Regental Professor, Deisenhofer accepted a position of an investigator at the Dallas unit of the Howard Hughes Medical Institute. Therein, he promoted the use of X-ray crystallography in the study of water-soluble proteins, membrane proteins, and other macromolecules and developed additional crystallographic software.
In 1993, he collaborated with fellow scientist James R. Norris of the Argonne National Laboratory writing the two-volume book, ‘The Photosynthetic Reaction Center’. The book was based on research originating from his Nobel Prize-winning investigation into photosynthesis.
Currently, Deisenhofer serves on the board of advisors of Scientists and Engineers for America. Also, he serves as a Professor at the Department of Biophysics at the University of Texas Southwestern Medical Center.
Awards & Achievements
Deisenhofer’s most promising achievement came in 1988 when he was bestowed with the prestigious Nobel Prize in Chemistry, along with his colleagues Hartmut Michel and Robert Huber for determining the structure for the photosynthetic reaction center.
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In 1986, he along with Hartmut Michel was bestowed with the American Physical Society's Biological Physics Prize.
In 1988, he was presented with Germany’s Otto-Bayer Prize.
He was honored with the Knight Commander's Cross of the German Order of Merit and the Bavarian Order of Merit.
He was conferred with honorary degrees from the most reputed institutions including Drury College of Springfield, Missouri, and Burdwan University of West Bengal, India.
From 1992, he was a fellow of the American Association for the Advancement of Science. Later in 2001, he was named an Argonne fellow.
He is a member of several scientific societies including American Crystallographic Association, the German and U.S affiliates of the Biophysical Society, the German Society for Biological Chemistry, the Protein Society and Academia Europaea, Sigma Xi. He was honored as a foreign associate of the U.S. National Academy of Sciences since 1997.
Additionally, he served on the University of Chicago board of governors for the Argonne National Laboratory
In 2002, he was inducted into the Texas Science Hall of Fame