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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
10                 Genes for non-heme, no-metal chloroperoxidases and haloalkane dehalogenases were the
11 se, soybean peroxidase, Caldariomyces fumago chloroperoxidase, and mushroom polyphenol oxidase-is muc
12 te NMR spectroscopy of the 67.5-kDa vanadium chloroperoxidase, at 14.1 T.
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
15 investigate the role of glutamic acid 183 in chloroperoxidase catalysis.
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
20              Resonance Raman measurements on chloroperoxidase compound II (CPO-II) reveal an isotope
21 and Mossbauer spectroscopy, we have examined chloroperoxidase compound II (CPO-II).
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
25                   Cytochrome P450 (P450) and chloroperoxidase (CPO) are thiolate-ligated haem protein
26                                              Chloroperoxidase (CPO) catalyzes the enantioselective ox
27 g x-ray absorption spectroscopy, we examined chloroperoxidase (CPO) compound I (CPO-I).
28                                              Chloroperoxidase (CPO) is suspected to play an important
29 py to study a heme-N-alkylated derivative of chloroperoxidase (CPO) prepared by mechanism-based inact
30            The heme active site structure of chloroperoxidase (CPO), a glycoprotein that displays ver
31 articles (MNPs) and electrostatic loading of chloroperoxidase (CPO).
32 e rebinding kinetics of Caldariomyces fumago chloroperoxidase (CPO).
33 o those observed in cytochrome P450(cam) and chloroperoxidase (CPO).
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.
37                                        Since chloroperoxidase functions normally through the ferric a
38                         Mutant clones of the chloroperoxidase genome have been expressed in a Caldari
39 d on the x-ray crystallographic structure of chloroperoxidase, Glu-183 is postulated to function on d
40         The presence of a thiolate ligand in chloroperoxidase has long been thought to play an essent
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
43                                              Chloroperoxidase, in addition to catalyzing classical pe
44                                              Chloroperoxidase is a versatile fungal heme-thiolate pro
45                                              Chloroperoxidase is a versatile heme enzyme which can cr
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
48                                  As eNOS and chloroperoxidase lie closer than do eNOS and P450cam on
49                       The vanadium-dependent chloroperoxidase Mcl24 was discovered to mediate a compl
50 he distal heme environment in eNOS resembles chloroperoxidase more than P450cam.
51                    The multiple functions of chloroperoxidase must be derived from its unique active
52 terization of a bacterial vanadium-dependent chloroperoxidase, NapH1 from Streptomyces sp. CNQ-525, w
53        The haloperoxidase Notomastus lobatus chloroperoxidase (NCPO) is unusual in requiring a flavop
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
56                                              Chloroperoxidase possesses a proximal cysteine thiolate
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
59  to the heme iron may be weaker, as found in chloroperoxidase, than in cytochrome P-450 enzymes.
60 ntained a previously described C. inaequalis chloroperoxidase that very likely catalyzed lignin chlor
61                 C. fumago produces wild-type chloroperoxidase, thus requiring gene replacement of the
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
64 r in the resting state of vanadium-dependent chloroperoxidases (VCPO).
65 acid phosphatases, and a vanadium-containing chloroperoxidase (whose tertiary structure is known) sha