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1 tified by mass spectrometry as calumenin and cytochrome B5.
2 in ActA or the endoplasmic reticulum protein cytochrome b5.
3 presence of an N-terminal domain related to cytochrome b5.
4 been purified to homogeneity and is soluble cytochrome b5.
5 to be involved in binding the heme domain of cytochrome b5.
6 ied that exhibited decreased ability to bind cytochrome b5.
7 s reduced differential absorbance spectra of cytochrome b5.
8 entical to the one elucidated for microsomal 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 the lyase reaction, even in the presence 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 s and revealed the transmembrane topology of cytochrome b5.
16 organ interval flanked by genes Cysteine and Cytochrome B5.
17 wo conserved side chain packing motifs in OM cytochrome b5s.
18 bilizing isomer A relative to isomer B in Mc cytochromes b5.
19 rkably different properties of rat OM and Mc cytochromes b5.
20 rd chemical and thermal denaturation than Mc cytochromes b5.
21 o acid sequence of the full-length house fly cytochrome b5 (134 residues) is 48% identical to that of
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
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
40 at the structures of bovine liver microsomal cytochrome b5 and rat liver OM cytochrome b5 are almost
42 nate from the formation of a complex between cytochrome b5 and the modified electrode surface which (
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
50 egrees C while the dissociation of heme from cytochrome b5 at room temperature occurs 3 orders of mag
53 Two acidic residues, Glu-48 and Glu-49, of cytochrome b5 (b5) are essential for stimulating the 17,
55 the need for the substrate testosterone and cytochrome b5 (b5) for reduction and as to whether reduc
58 amined are enhanced by the accessory protein cytochrome b5 (b5), but the exact role of b5 in P450 17A
68 , and in vitro plant systems have shown that cytochrome b5 can, at least in some circumstances, also
71 ) resonances were monitored as a function of cytochrome b5 concentration by 1H-15N TROSY-HSQC experim
72 The effector activity of the particular rat cytochrome b5 construct used for NMR studies was confirm
74 ins NADH-cytochrome b5 reductase (CYB5R) and cytochrome b5 (CYB5), it catalyzes the reduction of N-hy
75 finity (a Kd of 13 +/- 3 mM, for the reduced cytochrome b5-CYP-S-CO complex compared to a Kd of 26 +/
76 evious molecular dynamics (MD) simulation of cytochrome b5 (cyt b5) at 25 degrees C displayed localiz
77 (Mb) and its physiological partner protein, cytochrome b5 (cyt b5) can be "symmetrized": the [Mb:cyt
78 We report here on two such ET complexes: cytochrome b5 (cyt b5) in reaction with its physiologica
81 stigate localized dynamics on the surface of cytochrome b5 (cyt b5) that result in the formation of a
82 th membrane-bound P450 and its redox partner cytochrome b5 (cytb5 ) have been found to be important f
83 uentially delivered from its redox partners: cytochrome b5 (cytb5) and cytochrome P450 reductase, bot
85 ds that produce various heme proteins (e.g., cytochrome b5, cytochrome b562, and hemoglobin) in the p
86 formed on a solution containing a mixture of cytochrome b5, cytochrome c and polylysine, cytochrome b
88 tes that FA2H protein contains an N-terminal cytochrome b5 domain and four potential transmembrane do
89 de transmembrane sequences and a part of the cytochrome b5 domain are essential for the basal stabili
92 aliana FAH1 gene, which does not contain the cytochrome b5 domain, in the fah1Delta strain produced a
94 -affinity iron uptake system in an animal, a cytochrome b5 electron donor for ferric iron reduction,
95 tion potential (outer mitochondrial membrane cytochrome b5, Eo = -102 mV; microsomal cytochrome b5, E
96 rane cytochrome b5, Eo = -102 mV; microsomal cytochrome b5, Eo = 3 mV) in the presence of another pro
99 ochrome b5 reductase provides electrons, via cytochrome b5, for a range of biochemical reactions in c
100 can instead accept the second electron from cytochrome b5, for human steroidogenic CYP17A1, the cyto
101 ly demethylates m6A of targeted mRNA such as cytochrome b5 form A (CYB5A) to increase its mRNA stabil
105 yed by the outer mitochondrial membrane (OM) cytochrome b5 heme propionate groups in the electrostati
107 ntally, the interaction of cytochrome c with cytochrome b5 immobilized on a negatively charged monola
110 human P450-oxidoreductase (OR), and/or human cytochrome b5 in Saccharomyces cerevisiae and analyzed t
111 d out the conditional deletion of microsomal cytochrome b5 in the liver to create the hepatic microso
114 tion of P450c17 and the allosteric action of cytochrome b5 increase 17,20 lyase activity, but it has
115 sociation constant for manganese-substituted cytochrome b5 increased with temperature from 4 nM at 20
117 ), the dissociation of manganese substituted cytochrome b5 into the apoprotein and free Mn protoporph
118 indicates that the site of interaction on OM cytochrome b5 is almost identical to the one elucidated
122 conserved NAD(P)H reductase that contains a cytochrome b5-like domain at the N terminus and a cytoch
123 s two membrane-spanning domains as well as a cytochrome b5-like domain that is characteristic of nonm
124 accharomyces cerevisiae genome data base for cytochrome b5-like sequences identified a 1.152-kilobase
125 able effect on expression of CYP1A1, CYP2D6, cytochrome b5, liver or intestinal fatty acid binding pr
126 as much as 30% of the manganese-substituted cytochrome b5 may dissociate to free Mn-protoporphyrin I
127 rs a mechanism whereby allosteric binding of cytochrome b5 might selectively enhance the lyase reacti
132 50 enzymes showed that in hepatic microsomal cytochrome b5 null NADH-mediated metabolism was essentia
133 similar shifts in the reduction potential of cytochrome b5 occur when it forms a complex with physiol
134 mitochondrial membrane isoform of mammalian cytochrome b5 (OM b5) is considerably more stable than i
135 xial ligands in outer mitochondrial membrane cytochrome b5 (OM cyt b5) has been replaced by a methion
136 d in bacteria, human P450c17 required either cytochrome b5 or phosphorylation for 17,20 lyase activit
137 ion of both flavonoid 3',5'-hydroxylases and cytochrome b5 Overall, this work provides new insight in
139 onate located on the exposed heme edge of OM cytochrome b5 participates in the electrostatic binding
140 onate located on the exposed heme edge in OM cytochrome b5 participates in the electrostatic stabiliz
142 ic Iron Reductase) and Fire-like, as well as cytochrome b5 protein Firewood, are required for iron ab
145 osomal cytochrome P450 reductase and soluble cytochrome b5 reconstitute the activity of the porcine m
147 and the reducing systems, cytochrome b5 (B5)/cytochrome b5 reductase (B5R) and cytochrome P450 reduct
148 emia caused by an erythrocytic deficiency of cytochrome b5 reductase (b5R; type I) in African-America
152 er with the electron transport proteins NADH-cytochrome b5 reductase (CYB5R) and cytochrome b5 (CYB5)
153 asured in CHO cell lines overexpressing NADH:cytochrome b5 reductase (NBR), NADPH:cytochrome P450 red
154 ion of long chain fatty acids 7 (Elovl7) and cytochrome B5 reductase 2 (Cyb5r2) and the synaptic regu
158 s reduced to the Fe(2+) state by endothelial cytochrome b5 reductase 3 (CYB5R3, also known as diaphor
159 sights into NO-sGC-cGMP signaling and reveal cytochrome b5 reductase 3 as the first identified physio
161 in vascular smooth muscle cells reveal that cytochrome b5 reductase 3 expression and activity is cri
162 n and form protein-protein complexes between cytochrome b5 reductase 3, also known as methemoglobin r
164 anide reductase activity (indicative of NADH:cytochrome b5 reductase activity) coupled to inhibition
165 DNA insertional mutants of the gene encoding cytochrome b5 reductase in Arabidopsis thaliana, CBR1.
168 terminus of E3 to the N terminus of the NADH-cytochrome b5 reductase lacking the myristoyl group and
171 Interaction of Mtln with NADH-dependent cytochrome b5 reductase stimulates complex I functioning
175 hrome b5-like domain at the N terminus and a cytochrome b5 reductase-like domain at the C terminus.
183 eractions with the allosteric redox partner, cytochrome b5, required for CYP 17A1's lyase activity.
184 erric rat liver outer mitochondrial membrane cytochrome b5 (rOM b5) and ferric bovine liver microsoma
186 The X-ray crystal structure of rat liver OM cytochrome b5 solved to 2.7 A resolution shows that the
188 Dap1 is a heme-binding protein related to cytochrome b5 that activates Erg11, so that cells lackin
190 y acids, CER1-LIKE1 interacted with CER3 and cytochrome B5 to form a functional complex leading to th
191 sed amounts of POR, the allosteric action of cytochrome b5 to promote POR-P450c17 interaction, and Se
193 cytochrome b5, cytochrome c and polylysine, cytochrome b5 undergoes reversible electrochemistry at t
194 catalyzes the reduction of two molecules of cytochrome b5 using NADH as the physiological electron d
196 ctric constant on the reduction potential of cytochrome b5 was corroborated by preparing the V45L/V61
197 To achieve these aims, 13C-labeled heme OM cytochrome b5 was expressed in Escherichia coli as previ
201 rent K(m) for NADH increased; the K(m)'s for cytochrome b5 were unchanged relative to that of the wil
204 which is activated by a di-iron centre, and cytochrome b5, which regenerates the di-iron centre.
205 thionine synthase in the presence of soluble cytochrome b5 with a Vmax of 2.8 +/- 0.1 micromol min(-1