Cross-linked cytochrome P450 BM3 aggregates promoted by Ru(II)-diimine complexes bearing aldehyde groups

Cross-linked enzyme aggregate (CLEA) methodology has been applied to immobilize cytochrome P450 BM3 variants (F87A and 21B3) with peroxygenase activity. Several Ru(II)-diimine complexes were found to be suitable cross-linking agents, surpassing the traditional glutaraldehyde and dextran aldehyde. Th...

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Bibliographic Details
Published in:Journal of inorganic biochemistry 2018-09, Vol.186, p.130-134
Main Authors: Do, Minh Quan, Henry, Evelynn, Kato, Mallory, Cheruzel, Lionel
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Coordination Complexes - chemical synthesis
Coordination Complexes - chemistry
Cross-linked enzyme aggregates
Cross-Linking Reagents - chemistry
Cytochrome P-450 Enzyme System - chemistry
Enzymes, Immobilized - chemistry
Heterogeneous biocatalysis
Imines - chemistry
NADPH-Ferrihemoprotein Reductase - chemistry
P450 peroxygenase
Ru(II)-diimine complexes with aldehyde
Ruthenium - chemistry
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Summary:Cross-linked enzyme aggregate (CLEA) methodology has been applied to immobilize cytochrome P450 BM3 variants (F87A and 21B3) with peroxygenase activity. Several Ru(II)-diimine complexes were found to be suitable cross-linking agents, surpassing the traditional glutaraldehyde and dextran aldehyde. They offer modular numbers of aldehyde functionalities and a more rigid framework than their organic counterparts. The F87A CLEAs display significant activity loss compared to the protein in solution. Meanwhile, for the 21B3 CLEAs, high activity recovery (up to 95%) is obtained. In order to minimize enzyme leaching from the CLEA, sodium cyanoborohydride was used to reduce the CLEAs imine bonds. The reduced CLEAs were active for several rounds of reactions leading to an overall increase in protein activity of 170% compared to the free protein in solution. Several Ru(II)-diimine complexes bearing aldehyde moieties are suitable cross-linkers for the immobilization of cytochrome P450 BM3 variants. The heterogeneous biocatalyst peroxygenase activity often matches, and after several rounds of reactions, exceeds that of its homogeneous counterpart. [Display omitted] •Ru(II)-diimine complexes as cross-linking agent•Cross-linked cytochrome P450 BM3 aggregates with high peroxygenase activity recovery.•Heterogeneous biocatalysis
ISSN:0162-0134
1873-3344
DOI:10.1016/j.jinorgbio.2018.06.001