Light-driven Enzymatic Decarboxylation

Abstract

Oxidoreductases belong to the most-applied industrial enzymes. Nevertheless, they need external electrons whose supply is often costly and challenging. Recycling of the electron donors NADH or NADPH requires the use of additional enzymes and sacrificial substrates. Interestingly, several oxidoreductases accept hydrogen peroxide as electron donor. While being inexpensive, this reagent often reduces the stability of enzymes. A solution to this problem is the in situ generation of the cofactor. The continuous supply of the cofactor at low concentration drives the reaction without impairing enzyme stability. This paper demonstrates a method for the light-catalyzed in situ generation of hydrogen peroxide with the example of the heme-dependent fatty acid decarboxylase OleT JE . The fatty acid decarboxylase OleT JE was discovered due to its unique ability to produce long-chain 1-alkenes from fatty acids, a hitherto unknown enzymatic reaction. 1-alkenes are widely used additives for plasticizers and lubricants. OleT JE has been shown to accept electrons from hydrogen peroxide for the oxidative decarboxylation. While addition of hydrogen peroxide damages the enzyme and results in low yields, in situ generation of the cofactor circumvents this problem. The photobiocatalytic system shows clear advantages regarding enzyme activity and yield, resulting in a simple and efficient system for fatty acid decarboxylation.

Biochemical characterization of three new α-olefin-producing P450 fatty acid decarboxylases with a halophilic property

“…Nevertheless, the three new FADCs exhibited strong decarboxylation potentials and similar kinetic parameters to OleT JE . Future reaction process optimization such as in situ generation of H 2 O 2 [33, 34] or utilization of a redox cascade system [22, 26, 31] could be considered to attenuate the catalyst inactivation by high concentration H 2 O 2 .…”

“…Interestingly, OleT JE , the first identified P450 FADC remains the best biocatalyst for α-olefin production in terms of both catalytic efficiency and chemoselectivity (i.e., decarboxylation versus hydroxylation) when compared to other biochemically characterized P450 FADCs including P450 BSβ , CYP-MP, OleT MC , CYP-Aa162, and CYP-Sm46Δ29 [12, 19, 32]. Of note, some approaches such as redox partner engineering [31] and development of photocatalytic systems [33, 34] were also unsuccessful to improve the decarboxylation activity of OleT JE . Thus, it is highly expected to discover or engineer a novel CYP152 biocatalyst that can convert FFAs to 1-alkenes more efficiently and selectively.…”

Light-driven biocatalytic oxidation

“…5). The P450 fatty acid peroxygenases hydroxylate (or decarboxylate) saturated fatty acids (C 12 -C 20 ) [101][102][103] (Fig. 5a and b) The catalysis of CYP152L1 using this photochemical method was also applied to the conversion of uhydroxylated fatty acids (C 12 , C 15 , C 16 ), obtained from palm kernel oil, into the corresponding alkenols 104 (Fig.…”

“…Fig.5Photochemically driving P450 peroxygenases using FMN as a photocatalyst and EDTA as an electron donor. Hydroxylation of fatty acids[101][102][103] (a and b) and u-hydroxylated fatty acids 104 (c) is catalyzed by CYP152 peroxygenases. CYP102A1 heme domain also shows peroxygenase activity towards 4-nitrophenol (d) and lauric acid (e) 12.…”

Environmentally benign solid catalysts for sustainable biodiesel production: A critical review

“…One of the major problems in biodiesel synthesis via transesterification is the presence of high oxygen content in the final product which leads to lower energy content and limits its uses in applications requiring high energy density such as compression ignition engines. In this perspective, we are actively looking for alternatives, particularly by decarboxylation, to produce diesel like hydrocarbon fuels with enzymes (Köninger et al, 2016;Sorigué et al, 2017;Huijbers et al, 2018;Ma et al, 2020).…”