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1 in ActA or the endoplasmic reticulum protein cytochrome b5.
2  presence of an N-terminal domain related to cytochrome b5.
3  been purified to homogeneity and is soluble cytochrome b5.
4 to be involved in binding the heme domain of cytochrome b5.
5 ied that exhibited decreased ability to bind cytochrome b5.
6 s reduced differential absorbance spectra of cytochrome b5.
7 entical to the one elucidated for microsomal cytochrome b5.
8  the lyase reaction, even in the presence of cytochrome b5.
9 m the heme propionate carbonyl carbons in OM cytochrome b5.
10 ) is 48% identical to that of rat microsomal cytochrome b5.
11 s and revealed the transmembrane topology of cytochrome b5.
12 g the several reactions that utilize reduced cytochrome b5.
13 e for interprotein electron self-exchange in cytochrome b5.
14 s, catalyzes the NADH-dependent reduction of cytochrome b5.
15 organ interval flanked by genes Cysteine and Cytochrome B5.
16 tified by mass spectrometry as calumenin and cytochrome B5.
17 wo conserved side chain packing motifs in OM cytochrome b5s.
18 rd chemical and thermal denaturation than Mc cytochromes b5.
19 bilizing isomer A relative to isomer B in Mc cytochromes b5.
20 rkably different properties of rat OM and Mc cytochromes b5.
21 o acid sequence of the full-length house fly cytochrome b5 (134 residues) is 48% identical to that of
22                                              Cytochrome b5 (a soluble form lacking the 20-amino-acid
23                                              Cytochrome b5, a microsomal electron-transfer protein, e
24  (CYP101) induced by the soluble fragment of cytochrome b5, a nonphysiological effector of CYP101, we
25 oup of CYP101-bound camphor upon addition of cytochrome b5, a phenomenon also associated with the for
26 he presence of an equimolar concentration of cytochrome b5 and a 10-fold molar excess of NADPH-cytoch
27 % similarity to that of the yeast microsomal cytochrome b5 and a 35% identity and 54% similarity to t
28 ple of an animal flavohemoprotein containing cytochrome b5 and chrome b5 reductase cytodomains.
29 physiological interaction between microsomal cytochrome b5 and cytochrome c (recently reviewed) has i
30 ond-order electron transfer reaction between cytochrome b5 and cytochrome c has been studied by cycli
31 sured for the association between microsomal cytochrome b5 and cytochrome c, clearly indicates that t
32  studies indicate that the binding sites for cytochrome b5 and cytochrome P450 reductase are, as pred
33 teins known to be stable without heme (e.g., cytochrome b5 and hemoglobin apoprotein) are significant
34 oups in the electrostatic binding between OM cytochrome b5 and horse heart cytochrome c was investiga
35 atic stabilization of the complex between OM cytochrome b5 and horse heart cytochrome c.
36 itution with the electron transport proteins cytochrome b5 and NADH-cytochrome b5 reductase.
37 -component redox system comprised of soluble cytochrome b5 and P450 reductase.
38                                              Cytochrome b5 and phosphorylation enhance 17,20 lyase ac
39                           The combination of cytochrome b5 and phosphorylation was not additive.
40 at the structures of bovine liver microsomal cytochrome b5 and rat liver OM cytochrome b5 are almost
41 erized with respect to their ability to bind cytochrome b5 and support substrate oxidation.
42 nate from the formation of a complex between cytochrome b5 and the modified electrode surface which (
43  the removal of the membranous segments from cytochrome b5 and the NADH-cytochrome b5 reductase.
44 1 repeats, a structural motif in common with cytochrome b5, and a HECT domain in common with E6-AP ub
45 orming an electron transfer chain with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductas
46 with insect NADPH cytochrome P450 reductase, cytochrome b5, and NADPH, the purified CYP4C7 metabolize
47 er microsomal cytochrome b5 and rat liver OM cytochrome b5 are almost identical when compared at medi
48 yme systems, we now show that the actions of cytochrome b5 are independent of the state of P450c17 ph
49                    Identification of soluble cytochrome b5 as a member of the reductive activation sy
50 egrees C while the dissociation of heme from cytochrome b5 at room temperature occurs 3 orders of mag
51                                              Cytochrome b5 augments the 17,20-lyase activity of cytoc
52 mals, a flavohemoprotein (b5+b5R) containing cytochrome b5 (b5) and b5 reductase (b5R) domains.
53   Two acidic residues, Glu-48 and Glu-49, of cytochrome b5 (b5) are essential for stimulating the 17,
54                    The membrane heme protein cytochrome b5 (b5) can enhance, inhibit, or have no effe
55  the need for the substrate testosterone and cytochrome b5 (b5) for reduction and as to whether reduc
56 ncreasing ionic strength and the presence of cytochrome b5 (b5) on these two systems.
57                                              Cytochrome b5 (b5) stimulates the rate of the 17,20-lyas
58 amined are enhanced by the accessory protein cytochrome b5 (b5), but the exact role of b5 in P450 17A
59 trates, and binding of the soluble domain of cytochrome b5 (b5).
60                                              Cytochrome b5 binding to CYP17A1 is also mutually exclus
61               We have found that Dap1p, like cytochrome b5, binds to heme and that Dap1p targets the
62  (rOM b5) and ferric bovine liver microsomal cytochrome b5 (bMc b5).
63 s to synthesize the Saccharomyces cerevisiae cytochrome b5 by using both LCR and assembly PCR.
64 f full-length microsomal cytochrome-P450 and cytochrome-b5 by solid-state NMR spectroscopy.
65            The small heme-containing protein cytochrome b5 can facilitate, inhibit, or have no effect
66          These data indicate that microsomal cytochrome b5 can play a major role in the in vivo metab
67 , and in vitro plant systems have shown that cytochrome b5 can, at least in some circumstances, also
68                                 A microsomal cytochrome b5 cDNA from the house fly, Musca domestica,
69 ull-length mammalian 72-kDa cytochrome P450-cytochrome b5 complex in lipid bilayers.
70 ) resonances were monitored as a function of cytochrome b5 concentration by 1H-15N TROSY-HSQC experim
71  The effector activity of the particular rat cytochrome b5 construct used for NMR studies was confirm
72      In vitro studies have demonstrated that cytochrome b5 (Cyb5) also modulates P450 function.
73 ins NADH-cytochrome b5 reductase (CYB5R) and cytochrome b5 (CYB5), it catalyzes the reduction of N-hy
74 finity (a Kd of 13 +/- 3 mM, for the reduced cytochrome b5-CYP-S-CO complex compared to a Kd of 26 +/
75 evious molecular dynamics (MD) simulation of cytochrome b5 (cyt b5) at 25 degrees C displayed localiz
76  (Mb) and its physiological partner protein, cytochrome b5 (cyt b5) can be "symmetrized": the [Mb:cyt
77     We report here on two such ET complexes: cytochrome b5 (cyt b5) in reaction with its physiologica
78                                              Cytochrome b5 (cyt b5) is a membrane-anchored electron-c
79                                    Mammalian cytochrome b5 (cyt b5) is a membrane-bound protein capab
80 stigate localized dynamics on the surface of cytochrome b5 (cyt b5) that result in the formation of a
81 th membrane-bound P450 and its redox partner cytochrome b5 (cytb5 ) have been found to be important f
82 uentially delivered from its redox partners: cytochrome b5 (cytb5) and cytochrome P450 reductase, bot
83                                   Microsomal cytochrome b5 (cytb5) is a membrane-bound protein that m
84 ds that produce various heme proteins (e.g., cytochrome b5, cytochrome b562, and hemoglobin) in the p
85 formed on a solution containing a mixture of cytochrome b5, cytochrome c and polylysine, cytochrome b
86                                              Cytochrome b5 decreases the apparent Km for P450 reducta
87 tes that FA2H protein contains an N-terminal cytochrome b5 domain and four potential transmembrane do
88 de transmembrane sequences and a part of the cytochrome b5 domain are essential for the basal stabili
89                  FA2H lacking the N-terminal cytochrome b5 domain had little activity, indicating tha
90         Expression of the S. cerevisiae FAH1 cytochrome b5 domain in Escherichia coli produces a solu
91 aliana FAH1 gene, which does not contain the cytochrome b5 domain, in the fah1Delta strain produced a
92 84-amino acid protein with an amino-terminal cytochrome b5 domain.
93 tion potential (outer mitochondrial membrane cytochrome b5, Eo = -102 mV; microsomal cytochrome b5, E
94 rane cytochrome b5, Eo = -102 mV; microsomal cytochrome b5, Eo = 3 mV) in the presence of another pro
95                        Two distinct forms of cytochrome b5 exist in the rat hepatocyte.
96                                  Suppressing cytochrome b5 expression in human adrenal NCI-H295A cell
97 ochrome b5 reductase provides electrons, via cytochrome b5, for a range of biochemical reactions in c
98  can instead accept the second electron from cytochrome b5, for human steroidogenic CYP17A1, the cyto
99 ectroscopy reveal properties very similar to cytochromes b5 from vertebrates.
100                     In erythrocytes, soluble cytochrome b5 functions in methemoglobin reduction.
101 orientation on electrochemical properties of cytochrome b5 have been performed.
102 yed by the outer mitochondrial membrane (OM) cytochrome b5 heme propionate groups in the electrostati
103                                         Anti-cytochrome b5 IgG decreased NADPH- and NADH-dependent HE
104 ntally, the interaction of cytochrome c with cytochrome b5 immobilized on a negatively charged monola
105               Interestingly, the addition of cytochrome b5 improved the coupling of the mutant, resul
106 at of NADPH, and assess the possible role of cytochrome b5 in HER formation.
107 human P450-oxidoreductase (OR), and/or human cytochrome b5 in Saccharomyces cerevisiae and analyzed t
108 d out the conditional deletion of microsomal cytochrome b5 in the liver to create the hepatic microso
109                             The inclusion of cytochrome b5 in the reconstituted enzyme system is with
110                             The inclusion of cytochrome b5 in the reconstituted system of 2D6 and 2C9
111 tion of P450c17 and the allosteric action of cytochrome b5 increase 17,20 lyase activity, but it has
112 sociation constant for manganese-substituted cytochrome b5 increased with temperature from 4 nM at 20
113         The resonance Raman spectrum of MnII cytochrome b5 indicated a high-spin pentacoordinate stru
114 ), the dissociation of manganese substituted cytochrome b5 into the apoprotein and free Mn protoporph
115 indicates that the site of interaction on OM cytochrome b5 is almost identical to the one elucidated
116              When the reduction potential of cytochrome b5 is measured with the aid of several differ
117                                          The cytochrome b5 is reduced by house fly cytochrome P450 re
118 3 (CER3) and endoplasmic reticulum-localized cytochrome b5 isoforms (CYTB5s).
119  conserved NAD(P)H reductase that contains a cytochrome b5-like domain at the N terminus and a cytoch
120 s two membrane-spanning domains as well as a cytochrome b5-like domain that is characteristic of nonm
121 accharomyces cerevisiae genome data base for cytochrome b5-like sequences identified a 1.152-kilobase
122 able effect on expression of CYP1A1, CYP2D6, cytochrome b5, liver or intestinal fatty acid binding pr
123  as much as 30% of the manganese-substituted cytochrome b5 may dissociate to free Mn-protoporphyrin I
124 rs a mechanism whereby allosteric binding of cytochrome b5 might selectively enhance the lyase reacti
125                                    In vitro, cytochrome b5 modulates the rate of cytochrome P450-depe
126 and which constitutes part of the surface of cytochrome b5, modulates its reduction potential.
127  decreased by 3.6-fold in hepatic microsomal cytochrome b5 null mice.
128 n the liver to create the hepatic microsomal cytochrome b5 null mouse.
129 50 enzymes showed that in hepatic microsomal cytochrome b5 null NADH-mediated metabolism was essentia
130 similar shifts in the reduction potential of cytochrome b5 occur when it forms a complex with physiol
131  mitochondrial membrane isoform of mammalian cytochrome b5 (OM b5) is considerably more stable than i
132 xial ligands in outer mitochondrial membrane cytochrome b5 (OM cyt b5) has been replaced by a methion
133 d in bacteria, human P450c17 required either cytochrome b5 or phosphorylation for 17,20 lyase activit
134 ion of both flavonoid 3',5'-hydroxylases and cytochrome b5 Overall, this work provides new insight in
135                                  The NAD(P)H cytochrome b5 oxidoreductase, Ncb5or (previously named b
136 onate located on the exposed heme edge of OM cytochrome b5 participates in the electrostatic binding
137 onate located on the exposed heme edge in OM cytochrome b5 participates in the electrostatic stabiliz
138                                The house fly cytochrome b5 protein was overexpressed in Escherichia c
139 ow-spin heme similar to those found in other cytochrome b5 proteins.
140 osomal cytochrome P450 reductase and soluble cytochrome b5 reconstitute the activity of the porcine m
141               The structure and stability of cytochrome b5 reconstituted with manganese protoporphyri
142 emia caused by an erythrocytic deficiency of cytochrome b5 reductase (b5R; type I) in African-America
143                                              Cytochrome b5 reductase (cb5r) (EC 1.6.6.2) catalyzes th
144                                              Cytochrome b5 reductase (cb5r), a member of the ferredox
145 gle base pair change in a gene encoding NADH:cytochrome b5 reductase (CBR1, At5g17770).
146 er with the electron transport proteins NADH-cytochrome b5 reductase (CYB5R) and cytochrome b5 (CYB5)
147 asured in CHO cell lines overexpressing NADH:cytochrome b5 reductase (NBR), NADPH:cytochrome P450 red
148 ion of long chain fatty acids 7 (Elovl7) and cytochrome B5 reductase 2 (Cyb5r2) and the synaptic regu
149                                         NADH cytochrome b5 reductase 3 (CYB5R3) is critical for reduc
150 s reduced to the Fe(2+) state by endothelial cytochrome b5 reductase 3 (CYB5R3, also known as diaphor
151 sights into NO-sGC-cGMP signaling and reveal cytochrome b5 reductase 3 as the first identified physio
152                Mechanistically, we show that cytochrome b5 reductase 3 directly reduces oxidized sGC
153  in vascular smooth muscle cells reveal that cytochrome b5 reductase 3 expression and activity is cri
154 n and form protein-protein complexes between cytochrome b5 reductase 3, also known as methemoglobin r
155                                         NADH:cytochrome b5 reductase activates the mitomycins to alky
156 anide reductase activity (indicative of NADH:cytochrome b5 reductase activity) coupled to inhibition
157 DNA insertional mutants of the gene encoding cytochrome b5 reductase in Arabidopsis thaliana, CBR1.
158                   The results implicate NADH:cytochrome b5 reductase in the differential bioactivatio
159                  These results indicate that cytochrome b5 reductase is not essential during vegetati
160 terminus of E3 to the N terminus of the NADH-cytochrome b5 reductase lacking the myristoyl group and
161                      In all eukaryotes, NADH:cytochrome b5 reductase provides electrons, via cytochro
162                                 Because NADH:cytochrome b5 reductase resides predominantly in the mit
163                     A cytosolic form of NADH:cytochrome b5 reductase was generated.
164                       The orientation of the cytochrome b5 reductase was reversed, from cytosolic to
165 y cell transfectants overexpressing rat NADH:cytochrome b5 reductase were generated.
166 hrome b5-like domain at the N terminus and a cytochrome b5 reductase-like domain at the C terminus.
167                                      An NADH:cytochrome b5 reductase-transfected clone expressed 9-fo
168 ous segments from cytochrome b5 and the NADH-cytochrome b5 reductase.
169 on transport proteins cytochrome b5 and NADH-cytochrome b5 reductase.
170 with NADH, cytochrome b5, and NADH-dependent cytochrome b5 reductase.
171 ced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase.
172 e binding, while membrane binding of control cytochrome b5 remained unaffected.
173 erric rat liver outer mitochondrial membrane cytochrome b5 (rOM b5) and ferric bovine liver microsoma
174                                              Cytochrome b5 seems to play a role in HER formation, mos
175  The X-ray crystal structure of rat liver OM cytochrome b5 solved to 2.7 A resolution shows that the
176                    The results indicate that cytochrome b5 stimulates a step following the first elec
177    Dap1 is a heme-binding protein related to cytochrome b5 that activates Erg11, so that cells lackin
178                           In the presence of cytochrome b5 the variant readily metabolized 17EE and w
179 sed amounts of POR, the allosteric action of cytochrome b5 to promote POR-P450c17 interaction, and Se
180  a possible route for electron transfer from cytochrome b5 to the di-iron centre.
181  cytochrome b5, cytochrome c and polylysine, cytochrome b5 undergoes reversible electrochemistry at t
182  catalyzes the reduction of two molecules of cytochrome b5 using NADH as the physiological electron d
183        The resonance Raman spectrum of MnIII cytochrome b5 was consistent with a high-spin hexacoordi
184 ctric constant on the reduction potential of cytochrome b5 was corroborated by preparing the V45L/V61
185   To achieve these aims, 13C-labeled heme OM cytochrome b5 was expressed in Escherichia coli as previ
186                               Interestingly, cytochrome b5 was found to dramatically inhibit both P45
187                                     Data for cytochrome b5 were analyzed and, when the self-associati
188                                   Mutants of cytochrome b5 were designed to achieve reorientation of
189 rent K(m) for NADH increased; the K(m)'s for cytochrome b5 were unchanged relative to that of the wil
190                          Dap1p is related to cytochrome b5, which activates cytochrome P450 proteins,
191                                              Cytochrome b5, which augments several P450 activities, i
192  which is activated by a di-iron centre, and cytochrome b5, which regenerates the di-iron centre.
193 thionine synthase in the presence of soluble cytochrome b5 with a Vmax of 2.8 +/- 0.1 micromol min(-1
194           Titrations of [13C]heme-labeled OM cytochrome b5 with horse heart cytochrome c were carried
195                           The association of cytochrome b5 with the reduced CYP101-camphor-carbon mon

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