16899-09-5Relevant academic research and scientific papers
A series of hybrid P450 BM3 enzymes with different catalytic activity in the light-initiated hydroxylation of lauric acid
Tran, Ngoc-Han,Huynh, Ngoc,Chavez, Garrett,Nguyen, Angelina,Dwaraknath, Sudharsan,Nguyen, Thien-Anh,Nguyen, Maxine,Cheruzel, Lionel
, p. 50 - 56,7 (2012)
We have developed a series of hybrid P450 BM3 enzymes to perform the light-activated hydroxylation of lauric acid. These enzymes contain a Ru(II)-diimine photosensitizer covalently attached to single cysteine residues of mutant P450 BM3 heme domains. The library of hybrid enzymes includes four non-native single cysteine mutants (K97C, Q397C, Q109C and L407C). In addition, mutations around the heme active site, F87A and I401P, were inserted in the Q397C mutant. Two heteroleptic Ru(II) complexes, Ru(bpy)2phenA (1) and Ru(phen)2phenA (2) (bpy = bipyridine, phen = 1,10-phenanthroline, and phenA = 5-acetamido-1,10-phenanthroline), are used as photosensitizers. Upon visible light irradiation, the hybrid enzymes display various total turnover numbers in the hydroxylation of lauric acid, up to 140 for the L407C-1 mutant, a 16-fold increase compared to the F87A/Q397C-1 mutant. CO binding studies confirm the ability of the photogenerated Ru(I) compound to reduce the fraction of ferric high spin species present in the mutants upon substrate binding.
ALKANE OXIDATION BY MODIFIED HYDROXYLASES
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Paragraph 0342, (2016/02/16)
This invention relates to modified hydroxylases. The invention further relates to cells expressing such modified hydroxylases and methods of producing hydroxylated alkanes by contacting a suitable substrate with such cells.
A self-sufficient peroxide-driven hydroxylation biocatalyst
Cirino, Patrick C.,Arnold, Frances H.
, p. 3299 - 3301 (2007/10/03)
Directed evolution of the heme domain of cytochrome P450 BM-3 has resulted in a versatile, highly active peroxide-driven hydroxylation catalyst (see picture) that requires neither NADPH nor reductase and functions in a cell-free reaction system. This simplified, biomimetic catalyst is amenable to further optimization, for example, to improve stability or alter its substrate range.
Regioselectivity and Activity of Cytochrome P450 BM-3 and Mutant F87A in Reactions Driven by Hydrogen Peroxide
Cirino, Patrick C.,Arnold, Frances H.
, p. 932 - 937 (2007/10/03)
Cytochrome P450 BM-3 (EC 1.14.14.1) is a monooxygenase that utilizes NADPH and dioxygen to hydroxylate fatty acids at subterminal positions. The enzyme is also capable of functioning as a peroxygenase in the same reaction, by utilizing hydrogen peroxide i
