Protein And Metal Complex Hybrids

November 2, 2021

How can chemical processes for the production of common chemicals be made more sustainable, environmentally friendly and economical than before? For example, without high temperatures and without organic solvents? The Leibniz Institute for Catalysis in Rostock has found an answer for the industrially significant hydroformation reaction. The institute uses a structurally modified enzyme that catalytically controls the production of aldehydes, important basic chemicals, under mild reaction conditions. This basic research is carried out within the framework of the Leibniz ComBioCat Scientific Campus.

Enzymes are biocatalysts that break down food components in organisms for optimal use. This occurs highly selectively, as well as at body temperature and under normal pressure. Researchers would also like to see such mild reaction conditions rather than harsh chemical processes, which in many cases still determine chemistry today.

Their goal is ‘green chemistry’, and the foundations for this are currently being laid in laboratories around the world. With the ComBioCat project, funded by the Leibniz Association with 1.13 million euros over four years, LIKAT chemist Prof. Dr. Paul Kamer (1960 – 2020) brought an exclusive scientific campus to the northeast.

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Less effort and resources

The campus will combine the expertise of all catalytic disciplines to develop biocatalysts and also chemocatalysts for the production of polymers, active medical ingredients and other basic and fine chemicals. “Its use would significantly reduce the effort and costs of chemical processes and save resources,” says PhD student Jan-Ole Moritz, who is doing his PhD at LIKAT on the catalytic reaction of alkenes to aldehydes.

Aldehydes are used on a large scale in solvents and preservatives, among other things, and as basic materials in the cosmetic industry. In the laboratory Jan-Ole Moritz takes as a starting material 1 octene, an alkene that is almost insoluble in water, which reacts in aqueous solution with carbon monoxide and hydrogen to form aldehydes. Industrially, this is done using a metal catalyst at a pressure of up to 100 bar and temperatures of up to 100 degrees Celsius, as well as an organic solvent. At Jan-Ole Moritz, an enzyme performs the task of the catalyst under much milder conditions.


The chemist has genetically engineered the enzyme with anchor points to which the catalyst component can attach itself: a metal supported by phosphorus ligands, the active center of the catalyst. Chemists refer to this combined reaction of classical bio- and chemical molecules to form an artificial metal-enzyme complex as bioconjugation. “The chemical properties of the metal core ensure the activity of the complex. The protein nature of the enzyme causes the high selectivity, ”says Jan-Ole Moritz.

He also explains what this means: “One of the special properties of the enzyme is its tunnel structure, for example. This makes it easy to pre-classify the starting molecules, so to speak. ‘ The tunnel forces the alkene molecules to a certain position with which they enter the reaction. This makes the process so selective because the final product is created exactly in the desired linear arrangement.

Molecular trap

The structure of the tunnel also helps Moritz, a doctoral student, to extend the limit of the reaction. In hydroforming, the starting materials dissolve in water. Only short chain alkenes with a maximum of three or four carbon atoms in the molecule are suitable for this. The more carbon atoms the alkenes contain, the more fat-loving they become, and therefore also more water-repellent. Therefore, they are useless for hydroforming: they do not dissolve. However, through the tunnel of the metal-enzyme complex, long-chain molecules with ten or twelve carbon atoms can also be attracted to the aqueous solution where they react with catalytic support.

For his work, Jan-Ole Moritz, who until now has mainly been at home in classical phosphorus chemistry, has acquired more typical techniques for biologists: the creation of cell cultures for the production of proteins and their harvesting, the modification genetics and purification, sterile work in accordance with the legal requirements of the Ordinance for the Protection of Genetic Engineering. LIKAT created a safety laboratory especially for this research.

Have the advantage

With these research topics, the Leibniz Institute for Catalysis, together with its three partners, the Leibniz Institute for Plasma Science and Technology and the two Pomeranian universities of Mecklenburg, secure a good position in a completely new field of research. In the future, metal-enzyme complexes will help, among other things, to develop processes for the use of biowaste for the production of basic materials and energy, an area in which LIKAT is already at the forefront. For researchers, the appeal of this Campus ComBioCat is to combine active principles from biology, chemistry and physics in order to replace oil and gas as a raw material base in the long term.

Dr. Loony Davis5
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Born and raised in Brussels in an English family, I have always lived in a multicultural environment. After several work experiences in marketing and communication, I came to Smart Water Magazine, which I describe as the most exciting challenge of my career.
I am a person with great restlessness and curiosity to learn, discover what I do not know, as well as reinvent myself daily, someone who is curious about life and wants to know. I enjoy sharing knowledge.
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