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1 is noncovalently complexed to resting state cytochrome c peroxidase.
2 scorbate peroxidase cation binding site into cytochrome c peroxidase.
3 sted as ligands for a cavity binding site in cytochrome c peroxidase.
4 on transfer akin to the axial Trp residue in cytochrome c peroxidase.
5 e biological role of LmP is to function as a cytochrome c peroxidase.
6 tyrosyl radical, analogous to Compound ES of cytochrome c peroxidase.
7 s in both yeast iso-1-cytochrome c and yeast cytochrome c peroxidase.
8 me c(550) fully occupies its binding site on cytochrome c peroxidase.
9 rement for reductive activation in bacterial cytochrome c peroxidases.
10 e N. europaea enzyme and compared with other cytochrome c peroxidases.
11 and dissimilar to those reported for diheme cytochrome c peroxidases.
12 ary solutions of horse cytochrome c bound to cytochrome c peroxidase act as targets for cytochrome c(
13 nary solutions of cytochrome c(550) bound to cytochrome c peroxidase act as targets for horse cytochr
14 ion, the SS-31/cardiolipin complex inhibited cytochrome c peroxidase activity, which catalyzes cardio
17 combination between Zn-porphyrin-substituted cytochrome c peroxidase and cytochrome c in single cryst
18 of horse cytochrome c to a binary complex of cytochrome c peroxidase and cytochrome c(550) and bindin
19 hemoglobin hybrids, (ii) the complex between cytochrome c peroxidase and cytochrome c, and (iii and i
20 ytochrome c550 for its binding to Paracoccus cytochrome c peroxidase and its delivery of the two elec
21 utron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; the
22 of alternative electron transfer pathways in cytochrome c peroxidase and may have useful applications
23 nd pseudoazurin bind at the same site on the cytochrome c peroxidase and that the pair of electrons r
24 nate the strong proximal hydrogen bonding in cytochrome c peroxidase and to introduce strong proximal
25 f horse ferricytochrome c with baker's yeast cytochrome c peroxidase and with six cytochrome c peroxi
26 mauG, exhibits sequence similarity to diheme cytochrome c peroxidases and is required for the synthes
27 ape routes in cytochrome P450 monooxygenase, cytochrome c peroxidase, and benzylsuccinate synthase (B
28 forms of myoglobin, horseradish peroxidase, cytochrome c peroxidase, and catalase deviate substantia
29 ecific receptor conformations of a cavity in cytochrome c peroxidase, and we confirm both ligand pose
30 und cytochrome c located on the back-side of cytochrome c peroxidase, approximately 180 degrees from
31 . cruzi heme-containing ascorbate peroxidase cytochrome c peroxidase (APx-CcP), an antioxidant enzyme
32 ms of myoglobin, horseradish peroxidase, and cytochrome c peroxidase are authentic iron(IV)oxos with
34 the stoichiometry of complex formation with cytochrome c peroxidase as studied by 1H-NMR spectroscop
35 del system Botrytis cinerea secretion of the cytochrome c-peroxidase, BcCcp1 removes plant-produced H
36 All known active forms of diheme bacterial cytochrome c peroxidase (bCcP) enzymes are described by
37 iheme enzymes MauG and BthA of the bacterial cytochrome c peroxidase (bCCP) superfamily produce an un
39 nH protein, a member of the bacterial diheme cytochrome c peroxidase (bCcP)/MauG superfamily, has bee
40 magnetic susceptibility tensors for free and cytochrome c peroxidase-bound iso-1-ferricytochrome c we
41 2 were in the order horseradish peroxidase > cytochrome c peroxidase (CcP) > soybean peroxidase > myo
43 structures for Compound II intermediates in cytochrome c peroxidase (CcP) and ascorbate peroxidase (
45 -linked complex between redox partners yeast cytochrome c peroxidase (CCP) and cytochrome c (cyt. c)
46 bits activities characteristic of both yeast cytochrome c peroxidase (CCP) and plant cytosolic ascorb
49 structure of the heme-containing peroxidase, cytochrome c peroxidase (CcP) at 1.5 and 3.0 kbar and ma
51 re, we report the 1.5-A crystal structure of cytochrome c peroxidase (CCP) compound I (CmpI) using da
52 sociated tryptophanyl radical that resembles cytochrome c peroxidase (Ccp) compound I were observed b
53 ions have been introduced into an engineered cytochrome c peroxidase (CcP) containing a Mn(II)-bindin
57 action between p-nitroperoxybenzoic acid and cytochrome c peroxidase (CcP) has been investigated as a
58 Tyr42, Tyr187, Tyr229, and Tyr236) in yeast cytochrome c peroxidase (CcP) has been probed by site-di
59 Forty-six charge-reversal mutants of yeast cytochrome c peroxidase (CcP) have been constructed in o
60 ngle-site charge-reversal mutations of yeast cytochrome c peroxidase (CcP) have been constructed to d
61 y structural components necessary to convert cytochrome c peroxidase (CcP) into a thiolate-ligated cy
63 electron transfer complex formed between the cytochrome c peroxidase (CCP) of Paracoccus denitrifican
64 converting three methionine residues in the cytochrome c peroxidase (CcP) proximal heme pocket to th
65 binding sites were created near the heme of cytochrome c peroxidase (CCP) such that one of the heme
66 orbate peroxidase (APX), was engineered into cytochrome c peroxidase (CcP) to test the hypothesis tha
68 er within complexes of cytochrome c (Cc) and cytochrome c peroxidase (CcP) was studied to determine w
69 lacement of the distal histidine, His-52, in cytochrome c peroxidase (CcP) with a lysine residue prod
70 the electrostatic complexes formed by yeast cytochrome c peroxidase (CCP) with horse cytochrome c (C
72 mily, notably ascorbate peroxidase (APX) and cytochrome c peroxidase (CcP), as well as a mitochondria
73 ned in a structurally nonhomologous protein, cytochrome c peroxidase (CcP), by only two mutations (Cu
74 utant lacking docA, which encodes a putative cytochrome c peroxidase (CCP), demonstrates up to a 10(5
75 s more sensitive to H(2)O(2) than mutants in cytochrome c peroxidase (ccp), methionine sulfoxide redu
76 stal histidine position on the properties of cytochrome c peroxidase (CcP), three CcP mutants in whic
77 ompared ligand binding to a buried cavity in Cytochrome c Peroxidase (CcP), where affinity is dominat
82 A member of class I heme peroxidases [TcAPx-cytochrome c peroxidase (CcP)], suggesting both ascorbat
83 orms of extensively deuterated S. cerevisiae cytochrome c peroxidase (CcP; EC 1.11.1.5) have been ove
87 ) complexes formed in solution by the cloned cytochrome c peroxidase [CcP(MI)] and cytochromes c from
89 CcP) with a lysine residue produces a mutant cytochrome c peroxidase, CcP(H52K), with spectral and ki
90 xponentially growing yeast, the heme enzyme, cytochrome c peroxidase (Ccp1) is targeted to the mitoch
92 al of 8 cells was dependent on mitochondrial cytochrome-c peroxidase (CCP1) and UTH1, present on chro
93 We have identified two substrates of Rbd1p: cytochrome c peroxidase (Ccp1p); and a dynamin-like GTPa
94 the structure of the one-to-one cytochrome c/cytochrome c peroxidase complex in solution exist: one i
95 lly defined interface, 201-213), (ii) the Zn-cytochrome c peroxidase complex with cytochrome c, [ZnCc
96 x between yeast iso-1-cytochrome c (yCc) and cytochrome c peroxidase compound I (CMPI) over a wide ra
97 the high- and low-affinity binding sites on cytochrome c peroxidase compound I (CMPI) was studied by
99 191 radical cation and the oxyferryl heme in cytochrome c peroxidase compound I inverted question mar
101 h-resolution crystal structure is available, cytochrome c peroxidase, despite the fact that the seque
103 xplains why, in the reaction with peroxides, cytochrome c peroxidase forms an amino acid-centered fre
106 l histidine deletion mutant, H175G, of yeast cytochrome c peroxidase has been an intriguing but unres
107 capture surface for small cytochromes on the cytochrome c peroxidase has implications for rate enhanc
108 ely 20%, LiP has four disulfide bonds, while cytochrome c peroxidase has none, and LiP is larger (343
109 he most striking difference is that, whereas cytochrome c peroxidase has tryptophans contacting the d
110 ral well characterized heme proteins such as cytochrome c peroxidase, horseradish peroxidase, and man
111 cs simulations of the W191G cavity mutant of cytochrome c peroxidase in explicit water reveal distinc
112 h cytochrome c peroxidase (CcP) and a mutant cytochrome c peroxidase in which the distal histidine ha
113 d the homologous plant peroxidases and yeast cytochrome c peroxidase, in its reactions with peroxides
114 the crystal structure of the H175G mutant of cytochrome c peroxidase, in which the histidine tether b
115 g of compounds to the W191G cavity mutant of cytochrome c peroxidase is characterized by X-ray crysta
118 ing the catalytic cycle, the proximal Trp in cytochrome c peroxidase is oxidized to a cation radical.
119 al Trp in ascorbate peroxidase but absent in cytochrome c peroxidase is thought to be one reason why
120 that the electrochemistry of the N. europaea cytochrome c peroxidase is unlike other peroxidases stud
121 A gonococcal catalase mutant and a catalase, cytochrome C peroxidase mutant exhibited greater suscept
124 easing cytochrome c binding affinity for the cytochrome c peroxidase mutants is consistent with the c
125 inding affinity between cytochrome c and the cytochrome c peroxidase mutants varies from no significa
127 shows that the cation-containing mutants of cytochrome c peroxidase no longer form a stable Trp radi
128 ng to the model proposed in previous papers, cytochrome c peroxidase of Paracoccus denitrificans can
129 for the binding of small cytochromes to the cytochrome c peroxidase of Paracoccus denitrificans.
130 ion in neurological models, and also reduces cytochrome c peroxidase production in neurodegenerative
131 ion in neurological models, and also reduces cytochrome c peroxidase production in neurodegenerative
132 pin and low-spin forms of recombinant native cytochrome c peroxidase (rCcP) and its His52 --> Leu var
133 s between recombinant yeast cytochrome c and cytochrome c peroxidase (rCcP) were synthesized via disu
134 ast iso-1-cytochrome c and recombinant yeast cytochrome c peroxidase (rCcP), in which the crystallogr
135 ets of myeloperoxidase and the nonhomologous cytochrome c peroxidase suggest that they may have simil
136 nt of Ctb is surprisingly similar to that of cytochrome c peroxidase, suggesting a role of Ctb in per
137 eme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generati
139 heme active site structure of an engineered cytochrome c peroxidase that closely mimics manganese pe
140 550) and binding of cytochrome c(550) to the cytochrome c peroxidase that is affected little by the p
141 ponent, and another gene encoding a putative cytochrome c peroxidase that may function to reduce peri
142 distinct from that of the homologous diheme cytochrome c peroxidases that require a mixed valence st
143 en compared with those of ferrous H175CD235L cytochrome c peroxidase to show that its proximal ligand
144 es compared to c-type cytochromes and diheme cytochrome c peroxidases, to which it has some sequence
146 in which cytochrome c550, pseudoazurin, and cytochrome c peroxidase were all present could be modele
147 nt genes catalase, superoxide dismutase, and cytochrome c peroxidase were more sensitive to the letha
148 roxidase is the tryptophan cation radical in cytochrome c peroxidase which exhibits a g tensor with g
149 results reveal that TcAPx-CcP is a credible cytochrome c peroxidase, which can also bind and use asc
150 ibe here a reaction catalyzed by a mutant of cytochrome c peroxidase, which is similar but distinct f
151 crystals of yeast zinc porphyrin substituted cytochrome c peroxidase (ZnCcP) in complex with yeast is