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1 und I derivative of the heme-thiolate enzyme chloroperoxidase.
2 rom the two-electron oxidations catalyzed by chloroperoxidase.
3 the chlorination and dismutation activity of chloroperoxidase.
4 t essential for the chlorination activity of chloroperoxidase.
5 nd had significant overlap with complexes of chloroperoxidase.
6 for compound I of horseradish peroxidase and chloroperoxidase.
7 f which putatively encode vanadium-dependent chloroperoxidases.
8 ve-site alignment of the vanadium-containing chloroperoxidase and G6Pases predicts that Arg-83, His-1
9 nplay the importance of a thiolate ligand in chloroperoxidase and suggest that the distal environment
11 se, soybean peroxidase, Caldariomyces fumago chloroperoxidase, and mushroom polyphenol oxidase-is muc
13 t investigation, ferric and ferrous alkaline chloroperoxidase (C420) have been characterized by elect
14 dase (MPO), eosinophil peroxidase (EPO), and chloroperoxidase can oxidize iodide, bromide, and chlori
16 dative dehalogenation catalyzed by C. fumago chloroperoxidase (CCPO) involves two consecutive one-ele
17 f suitable amounts of peroxide and chloride, chloroperoxidase chlorinates thionin and bleaches the in
18 r spectrum of CYP119-I is similar to that of chloroperoxidase compound I, although its electron param
19 roscopy, we have found that the Fe-O bond in chloroperoxidase compound II (CPO-II) is much longer tha
22 n explicitly solvated cis-beta-methylstyrene/chloroperoxidase-Compound I complex are performed to det
23 ymatic natural halogenation: chlorination by chloroperoxidase (CPO) and flavin-dependent halogenases
24 dependent peroxidatic reactions catalyzed by chloroperoxidase (CPO) are extended to CPO-catalyzed hal
29 py to study a heme-N-alkylated derivative of chloroperoxidase (CPO) prepared by mechanism-based inact
34 cid residue supplying the thiolate ligand in chloroperoxidase, Cys-29 has been replaced with a histid
35 ith different reactivities toward C-H bonds: chloroperoxidase, cytochrome P450, and a selenolate (sel
36 two algal bromoperoxidases and the vanadium chloroperoxidase from the fungus Curvularia inaequalis.
39 d on the x-ray crystallographic structure of chloroperoxidase, Glu-183 is postulated to function on d
41 on by representative soil enzymes (C. fumago chloroperoxidase, horseradish peroxidase, and laccase fr
42 eAPO-I (361, 694 nm) are similar to those of chloroperoxidase-I and the recently described cytochrome
46 ism by which the heme-containing peroxidase, chloroperoxidase, is able to chlorinate substrates is po
47 e spectroscopically related inactive form of chloroperoxidase lead to the conclusion that a sulfur-de
52 terization of a bacterial vanadium-dependent chloroperoxidase, NapH1 from Streptomyces sp. CNQ-525, w
54 H<=8.5) reproduces well the heme ligation in chloroperoxidases or cyt P450 monooxygenases and peroxid
55 pH 8.5) reproduces well the heme ligation in chloroperoxidases or cyt P450 monooxygenases and peroxid
57 tochromes; however, unlike the P450 enzymes, chloroperoxidase possesses a very polar environment dist
58 ponents of the global chlorine cycle because chloroperoxidase-producing fungi are ubiquitous in decay
60 ntained a previously described C. inaequalis chloroperoxidase that very likely catalyzed lignin chlor
62 This finding biochemically links a vanadium chloroperoxidase to microbial natural product biosynthes
63 In particular, under alkaline conditions, chloroperoxidase undergoes a transition to a new, spectr
65 acid phosphatases, and a vanadium-containing chloroperoxidase (whose tertiary structure is known) sha