In the earliest stages of life, cells mastered crucial chemical reactions like electron transfers, which are essential for building carbon—and nitrogen-based compounds. These reactions depend on enzymes with metal atom clusters.
MIT’s Associate Professor Daniel Suess is studying these enzymes to uncover methods for capturing atmospheric carbon and creating sustainable alternative fuels, offering hope for innovative climate solutions.
Professor Daniel Suess emphasizes the urgent need to shift society away from reliance on fossil fuels and carbon combustion. To achieve this, his approach involves looking deep into Earth’s ancient biochemical history—up to a billion years before photosynthesis and oxygen were prevalent.
By uncovering the chemical principles of early cellular processes, he aims to identify sustainable alternatives to carbon-burning methods, offering hope for a greener future.
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While at UC Davis, Daniel Suess transitioned into studying biomolecules, focusing on metalloproteins—enzymes with metal-containing active sites that drive crucial reactions. One enzyme of particular interest was iron-iron hydrogenase, found primarily in anaerobic bacteria, including some in the human gut.
This enzyme facilitates the transfer of protons and electrons, enabling it to either generate hydrogen gas (H2) from protons and electrons or split H2 into its components. This research deepened the understanding of how cells create these metal-containing active sites and the essential reactions they catalyze.
“That enzyme is really important because a lot of cellular metabolic processes either generate excess electrons or require excess electrons. If you generate excess electrons, they have to go somewhere, and one solution is to put them on protons to make H2,” Suess says.
After joining MIT in 2017, Daniel Suess deepened his research into metalloproteins and the vital reactions they facilitate. He focuses on global-scale chemical reactions—microscopic processes that occur on a vast scale and shape the molecular makeup of our planet.
These reactions, crucial to understanding Earth’s biosphere, hold the potential to influence its future composition and drive sustainable innovations.
Photosynthesis transformed the Earth’s atmosphere 2.4 billion years ago by producing oxygen, but Daniel Suess focuses on even older cellular reactions from a time when life thrived without oxygen.
These ancient processes, still active in modern cells, often involve iron-sulfur metalloproteins, which handle challenging reactions like forming carbon radicals or converting nitrogen gas into ammonia.
To study these enzymes, Suess’s lab employs two strategies: creating synthetic versions with simplified structures for controlled analysis or using natural proteins altered with isotopes to enable detailed spectroscopic studies.
This work enhances understanding of enzyme functions and could lead to breakthroughs in carbon capture and greener nitrogen-to-ammonia conversion, addressing critical environmental challenges.
By unraveling how these ancient biochemical pathways operate, Suess aims to discover sustainable solutions to reduce greenhouse gas emissions and harness nature’s chemistry for modern needs.
