Biological halogenation: roles in nature, potential in industry

Spectroscopic characterization of the ferric states of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase: His-ligated peroxidases with globin-like proximal and distal properties

“…This makes DHP the first example of a peroxidase with a globin fold and the only known, enzymatically active globin [16]. NCPO belongs to a sub-family of peroxidase enzymes that use halide ions to halogenate organic substrates in a hydrogen peroxide-dependent manner [22][23][24]. The enzyme (M r $ 174,000) is composed of two separable protein moieties, a flavoprotein (FAD-bound, M r $ 120,000) with four identical subunits and a heme protein (M r $ 54,000) with two copies each of two subunits (M r $ 11,500 and 15,500); the complete system is necessary for haloperoxidase activity [8].…”

Isolation, biochemical and molecular characterization of 2-chlorophenol-degrading Bacillus isolates

“…A range of chlorinated organic compounds including chlorophenols can be produced by biologic chlorination as well (Neidleman and Geigert, 1986). Therefore, in the last few years, contamination of the environment by chlorinated aromatic compounds has been the subject of increased concern.…”

Theoretical Study of Chloroperoxidase Catalyzed Chlorination of beta-Cyclopentanedione and Role of Water in the Chlorination Mechanism

“…However, its most prominent reaction, chlorination, is still not completely understood. One postulated mechanism involves catalytic formation of HOCl at the active site of CPO followed by release into solution, where it halogenates substrates [4,[15][16][17][18][19][20][21]. The other postulated mechanism involves the chlorination of substrates at the heme active site [22][23][24][25][26][27][28][29][30].…”

“…Since being discovered more than 50 years ago, CPO has been studied extensively because of its versatility, ecological significance and potential applicability in the pharmaceutical industry [4].…”

“…A ( C2 -C3 -H31 3b3 2 3 6 8 0 !24 A11 A (3,6,8) C2 -C3 -H32 3b4 2 3 6 9 0 !25 A12 A (3,6,9) C2 -C3 -C4 r1a1 gamma 2 7 6 8 0 !26 A13 A (7,6,8) H31 -C3 -H32 3 alpha 2 7 6 9 0 !27 A14 A (7,6,9) H31 -C3 -C4 3b1 2 8 6 9 0 !28 A15 A (8,6,9) H32 -C3 -C4 3b2 2 6 9 10 0 !29 A16 A(6,9,10) C3 -C4 -O4 4b1 2 6 9 11 0 !30 A17 A (6,9,11) C3 -C4 -C5 r1a2 2 10 9 11 0 !31 A18 A(10,9,11) O4 -C4 -C5 4b2 2 1 11 9 0 !32 A19 A (1,11,9) C1 -C5 -C4 r1a3 gamma 2 1 11 12 0 !33 A20 A(1,11,12) C1 -C5 -H51 5b1 2 1 11 13 0 !34 A21 A(1,11,13) C1 -C5 -H52 5b2 2 9 11 12 0 !35 A22 A(9,11,12) C4 -C5 -H51 5b3 2 9 11 13 0 !36 A23 A(9,11,13) C4 -C5 -H52 5b4 2 12 11 13 0 !37 A24 A(12,11,13) H51 -C5 -H52 5 alpha 3 1 3 11 2 !38 I1 I(1,3,11,2) C1-C2-C5-O1 C1 3 9 11 6 10 !39 I1 I(9,11,6,10) C5-C1-C2-O4 C4 4 11 1 3 6 !40 D1 D(11,1,3,6) C5-C1-C2-C3 r1t4 4 1 3 6 9 !41 D2 D(1,3,6,9) C1-C2-C3-C4 r1t5 4 3 6 9 11 !42 D3 D(3,6,9,11) C2-C3-C4-C5 r1t1 4 6 9 11 1 !43 D4 D(6,9,11,1) C3-C4-C5-C1 r1t2 4 C2 -C3 -H31 3b3 2 3 6 8 0 !24 A11 A (3,6,8) C2 -C3 -H32 3b4 2 3 6 9 0 !25 A12 A (3,6,9) C2 -C3 -C4 r1a1 gamma 2 7 6 8 0 !26 A13 A (7,6,8) H31 -C3 -H32 3 alpha 2 7 6 9 0 !27 A14 A (7,6,9) H31 -C3 -C4 3b1 2 8 6 9 0 !28 A15 A (8,6,9) H32 -C3 -C4 3b2 2 6 9 10 0 !29 A16 A(6,9,10) C3 -C4 -O4 4b1 2 6 9 11 0 !30 A17 A …”