Nature is the perfect epitome of design. Chemists often draw inspiration from nature when designing catalysts for many chemical reactions. Biochemists study the natural biological system to understand why and how nature does every reaction so efficiently. As an inorganic chemist, one of my favorite reactions is electron transfer. Rudolph Marcus developed a theory of electron transfer, which later led him to single-handedly won a Nobel prize in chemistry in 1992.1 In his theory, an electron transfers from a donor to an acceptor with a specific rate, which is maximized at an optimal specific energetic driving force. A driving force too small leads to slow electron transfer. A driving force too large also leads to slow electron transfer. There exists an optimal driving force of which electron can transfer without a barrier.
Nature elegantly optimizes electron transfer process, the most important reaction of which happens in respiration. The membrane of mitochondria consists of Complex I, a protein complex which facilitate electron and proton transfer processes with remarkable efficiency. Key to this low activation barrier process is the careful arrangement of iron-sulfur clusters which serves as electron transport cofactors (Figure 1). In addition, Martin and Matyushov show through computational methods that hydration of these cofactors alter electrostatic and spin interactions leading to further lowering of the activation barrier according to Marcus theory.
Figure 1. Complex I. (a) Peripheral and membrane-bound parts of complex I. (b) Cofactors (yellow) involved in the electron transfer chain in the peripheral arm. Also shown are docked NAD+ and ubiquinone (Q). Figure reproduced from reference 2.
Needless to say, the design of Complex I is extremely complex, and one can deduce that such intricate design can merely derive from chances. Imagine a protein with 100 amino acids, the probability of forming a protein of the correct sequence by random is 1/20100, which is equal to 1 in 1.3x10130. Meanwhile, the estimated number of atoms in the universe is 1078-1082.3 It is thus inconceivable how a correct protein can be formed by random chance since there is simply not enough atoms to try all the possibilities even for a single protein.
Not only in a protein, but purposeful design can also be found in other systems, ranging from fundamental physical constants of the universe to the precise astronomical conditions of the earth to the irreducible complexities of living cells and more.4 Interested readers may find more information on these topics elsewhere.5
References
Electron Transfer Reactions in Chemistry: Theory and Experiment. Nobel Lecture. 8 December 1992. URL: https://www.nobelprize.org/prizes/chemistry/1992/marcus/lecture/
Martin, D. R.; Matyushov, D. V. "Electron-transfer chain in respiratory complex I". Scientific Reports, 2017, 7, 5495.
Villanueva, J. C. "How many atoms are there in the universe?" Universe Today, 30 July 2009. URL: https://www.universetoday.com/36302/atoms-in-the-universe
Penrose, R. “The Emperor’s New Mind” Oxford University Press, 1989.
Friederich, S. "Fine-Tuning", The Stanford Encyclopedia of Philosophy (Winter 2023 Edition), Edward N. Zalta & Uri Nodelman (eds.). URL: https://plato.stanford.edu/entries/fine-tuning