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1 is noncovalently complexed to resting state cytochrome c peroxidase.
2 e biological role of LmP is to function as a cytochrome c peroxidase.
3 scorbate peroxidase cation binding site into cytochrome c peroxidase.
4 tyrosyl radical, analogous to Compound ES of cytochrome c peroxidase.
5 s in both yeast iso-1-cytochrome c and yeast cytochrome c peroxidase.
6 me c(550) fully occupies its binding site on cytochrome c peroxidase.
7 sted as ligands for a cavity binding site in cytochrome c peroxidase.
8 rement for reductive activation in bacterial cytochrome c peroxidases.
9 e N. europaea enzyme and compared with other cytochrome c peroxidases.
10 and dissimilar to those reported for diheme cytochrome c peroxidases.
11 ary solutions of horse cytochrome c bound to cytochrome c peroxidase act as targets for cytochrome c(
12 nary solutions of cytochrome c(550) bound to cytochrome c peroxidase act as targets for horse cytochr
13 ion, the SS-31/cardiolipin complex inhibited cytochrome c peroxidase activity, which catalyzes cardio
16 combination between Zn-porphyrin-substituted cytochrome c peroxidase and cytochrome c in single cryst
17 of horse cytochrome c to a binary complex of cytochrome c peroxidase and cytochrome c(550) and bindin
18 hemoglobin hybrids, (ii) the complex between cytochrome c peroxidase and cytochrome c, and (iii and i
19 ytochrome c550 for its binding to Paracoccus cytochrome c peroxidase and its delivery of the two elec
20 utron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; the
21 of alternative electron transfer pathways in cytochrome c peroxidase and may have useful applications
22 nd pseudoazurin bind at the same site on the cytochrome c peroxidase and that the pair of electrons r
23 nate the strong proximal hydrogen bonding in cytochrome c peroxidase and to introduce strong proximal
24 f horse ferricytochrome c with baker's yeast cytochrome c peroxidase and with six cytochrome c peroxi
25 mauG, exhibits sequence similarity to diheme cytochrome c peroxidases and is required for the synthes
26 forms of myoglobin, horseradish peroxidase, cytochrome c peroxidase, and catalase deviate substantia
27 ecific receptor conformations of a cavity in cytochrome c peroxidase, and we confirm both ligand pose
28 und cytochrome c located on the back-side of cytochrome c peroxidase, approximately 180 degrees from
29 ms of myoglobin, horseradish peroxidase, and cytochrome c peroxidase are authentic iron(IV)oxos with
31 the stoichiometry of complex formation with cytochrome c peroxidase as studied by 1H-NMR spectroscop
32 All known active forms of diheme bacterial cytochrome c peroxidase (bCcP) enzymes are described by
33 magnetic susceptibility tensors for free and cytochrome c peroxidase-bound iso-1-ferricytochrome c we
34 2 were in the order horseradish peroxidase > cytochrome c peroxidase (CcP) > soybean peroxidase > myo
37 -linked complex between redox partners yeast cytochrome c peroxidase (CCP) and cytochrome c (cyt. c)
38 bits activities characteristic of both yeast cytochrome c peroxidase (CCP) and plant cytosolic ascorb
42 re, we report the 1.5-A crystal structure of cytochrome c peroxidase (CCP) compound I (CmpI) using da
43 sociated tryptophanyl radical that resembles cytochrome c peroxidase (Ccp) compound I were observed b
44 ions have been introduced into an engineered cytochrome c peroxidase (CcP) containing a Mn(II)-bindin
47 action between p-nitroperoxybenzoic acid and cytochrome c peroxidase (CcP) has been investigated as a
48 Tyr42, Tyr187, Tyr229, and Tyr236) in yeast cytochrome c peroxidase (CcP) has been probed by site-di
49 Forty-six charge-reversal mutants of yeast cytochrome c peroxidase (CcP) have been constructed in o
50 ngle-site charge-reversal mutations of yeast cytochrome c peroxidase (CcP) have been constructed to d
51 y structural components necessary to convert cytochrome c peroxidase (CcP) into a thiolate-ligated cy
53 electron transfer complex formed between the cytochrome c peroxidase (CCP) of Paracoccus denitrifican
54 converting three methionine residues in the cytochrome c peroxidase (CcP) proximal heme pocket to th
55 binding sites were created near the heme of cytochrome c peroxidase (CCP) such that one of the heme
56 orbate peroxidase (APX), was engineered into cytochrome c peroxidase (CcP) to test the hypothesis tha
58 er within complexes of cytochrome c (Cc) and cytochrome c peroxidase (CcP) was studied to determine w
59 lacement of the distal histidine, His-52, in cytochrome c peroxidase (CcP) with a lysine residue prod
60 the electrostatic complexes formed by yeast cytochrome c peroxidase (CCP) with horse cytochrome c (C
62 utant lacking docA, which encodes a putative cytochrome c peroxidase (CCP), demonstrates up to a 10(5
63 s more sensitive to H(2)O(2) than mutants in cytochrome c peroxidase (ccp), methionine sulfoxide redu
64 stal histidine position on the properties of cytochrome c peroxidase (CcP), three CcP mutants in whic
65 ompared ligand binding to a buried cavity in Cytochrome c Peroxidase (CcP), where affinity is dominat
69 A member of class I heme peroxidases [TcAPx-cytochrome c peroxidase (CcP)], suggesting both ascorbat
70 orms of extensively deuterated S. cerevisiae cytochrome c peroxidase (CcP; EC 1.11.1.5) have been ove
74 ) complexes formed in solution by the cloned cytochrome c peroxidase [CcP(MI)] and cytochromes c from
76 CcP) with a lysine residue produces a mutant cytochrome c peroxidase, CcP(H52K), with spectral and ki
77 xponentially growing yeast, the heme enzyme, cytochrome c peroxidase (Ccp1) is targeted to the mitoch
79 al of 8 cells was dependent on mitochondrial cytochrome-c peroxidase (CCP1) and UTH1, present on chro
80 We have identified two substrates of Rbd1p: cytochrome c peroxidase (Ccp1p); and a dynamin-like GTPa
81 the structure of the one-to-one cytochrome c/cytochrome c peroxidase complex in solution exist: one i
82 lly defined interface, 201-213), (ii) the Zn-cytochrome c peroxidase complex with cytochrome c, [ZnCc
83 x between yeast iso-1-cytochrome c (yCc) and cytochrome c peroxidase compound I (CMPI) over a wide ra
84 the high- and low-affinity binding sites on cytochrome c peroxidase compound I (CMPI) was studied by
86 191 radical cation and the oxyferryl heme in cytochrome c peroxidase compound I inverted question mar
88 h-resolution crystal structure is available, cytochrome c peroxidase, despite the fact that the seque
89 xplains why, in the reaction with peroxides, cytochrome c peroxidase forms an amino acid-centered fre
92 l histidine deletion mutant, H175G, of yeast cytochrome c peroxidase has been an intriguing but unres
93 capture surface for small cytochromes on the cytochrome c peroxidase has implications for rate enhanc
94 ely 20%, LiP has four disulfide bonds, while cytochrome c peroxidase has none, and LiP is larger (343
95 he most striking difference is that, whereas cytochrome c peroxidase has tryptophans contacting the d
96 ral well characterized heme proteins such as cytochrome c peroxidase, horseradish peroxidase, and man
97 cs simulations of the W191G cavity mutant of cytochrome c peroxidase in explicit water reveal distinc
98 h cytochrome c peroxidase (CcP) and a mutant cytochrome c peroxidase in which the distal histidine ha
99 d the homologous plant peroxidases and yeast cytochrome c peroxidase, in its reactions with peroxides
100 the crystal structure of the H175G mutant of cytochrome c peroxidase, in which the histidine tether b
101 g of compounds to the W191G cavity mutant of cytochrome c peroxidase is characterized by X-ray crysta
104 ing the catalytic cycle, the proximal Trp in cytochrome c peroxidase is oxidized to a cation radical.
105 al Trp in ascorbate peroxidase but absent in cytochrome c peroxidase is thought to be one reason why
106 that the electrochemistry of the N. europaea cytochrome c peroxidase is unlike other peroxidases stud
107 A gonococcal catalase mutant and a catalase, cytochrome C peroxidase mutant exhibited greater suscept
110 easing cytochrome c binding affinity for the cytochrome c peroxidase mutants is consistent with the c
111 inding affinity between cytochrome c and the cytochrome c peroxidase mutants varies from no significa
113 shows that the cation-containing mutants of cytochrome c peroxidase no longer form a stable Trp radi
114 ng to the model proposed in previous papers, cytochrome c peroxidase of Paracoccus denitrificans can
115 for the binding of small cytochromes to the cytochrome c peroxidase of Paracoccus denitrificans.
116 pin and low-spin forms of recombinant native cytochrome c peroxidase (rCcP) and its His52 --> Leu var
117 s between recombinant yeast cytochrome c and cytochrome c peroxidase (rCcP) were synthesized via disu
118 ast iso-1-cytochrome c and recombinant yeast cytochrome c peroxidase (rCcP), in which the crystallogr
119 ets of myeloperoxidase and the nonhomologous cytochrome c peroxidase suggest that they may have simil
120 nt of Ctb is surprisingly similar to that of cytochrome c peroxidase, suggesting a role of Ctb in per
122 heme active site structure of an engineered cytochrome c peroxidase that closely mimics manganese pe
123 550) and binding of cytochrome c(550) to the cytochrome c peroxidase that is affected little by the p
124 ponent, and another gene encoding a putative cytochrome c peroxidase that may function to reduce peri
125 distinct from that of the homologous diheme cytochrome c peroxidases that require a mixed valence st
126 en compared with those of ferrous H175CD235L cytochrome c peroxidase to show that its proximal ligand
127 es compared to c-type cytochromes and diheme cytochrome c peroxidases, to which it has some sequence
129 in which cytochrome c550, pseudoazurin, and cytochrome c peroxidase were all present could be modele
130 nt genes catalase, superoxide dismutase, and cytochrome c peroxidase were more sensitive to the letha
131 roxidase is the tryptophan cation radical in cytochrome c peroxidase which exhibits a g tensor with g
132 ibe here a reaction catalyzed by a mutant of cytochrome c peroxidase, which is similar but distinct f
133 crystals of yeast zinc porphyrin substituted cytochrome c peroxidase (ZnCcP) in complex with yeast is
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