ライフサイエンスコーパス: hemoprotein

1 the monooxygenase reaction catalyzed by this hemoprotein.

2 affinity of oxidized and reduced Pdx to the hemoprotein.

3 ytic degradation of the oxidatively modified hemoprotein.

4 of guanylate cyclase (sGC), a heterodimeric hemoprotein.

5 t, as in mammals, involves a redox-sensitive hemoprotein.

6 scherichia coli expressed purified HO-2 is a hemoprotein.

7 gests that oxygen tension may be sensed by a hemoprotein.

8 RmdA contains a PAS9 domain and is a hemoprotein.

9 ith the rate at which heme was lost from the hemoprotein.

10 perone catalyzing the insertion of heme into hemoproteins.

11 y employing mechanisms to utilize the host's hemoproteins.

12 reliant on the acquisition of iron from host hemoproteins.

13 es efficient acquisition of Fe from heme and hemoproteins.

14 s reported for other six-coordinate NO-bound hemoproteins.

15 uired for assimilation of iron from heme and hemoproteins.

16 terms of the axial His orientation in b-type hemoproteins.

17 fic for the heme in sGC versus that in other hemoproteins.

18 itochondria and cytoplasm, and deficiency of hemoproteins.

19 is is thought to be reutilized from cellular hemoproteins.

20 ES is proposed for this remarkable family of hemoproteins.

21 ron porphyrin in each oxidation state of the hemoproteins.

22 variety of biological functions mediated by hemoproteins.

23 only for the formation of cytochrome c-type hemoproteins.

24 g tyrosine common to the NEAT superfamily of hemoproteins.

25 tween the cell wall associated IsdA and IsdC hemoproteins.

26 stage without apparent dysfunction of major hemoproteins.

27 he selective ligand responses in gas-sensing hemoproteins.

28 hus enabling electron transfer between these hemoproteins.

29 catalases, cytochromes, and other bacterial hemoproteins.

30 ates is in the form of heme as a cofactor of hemoproteins.

31 dicated to the acquisition of heme from host hemoproteins.

32 ct the regulation and physiology of cellular hemoproteins.

33 ized cytochrome P450s or by catalase-related hemoproteins.

34 avenge the essential nutrient iron from host hemoproteins.

35 in interactions between apoIsdC and upstream hemoproteins.

36 ransfer as well as a structural component of hemoproteins.

37 to identify trends in the architecture of b hemoproteins.

38 , is similar to that of other monotyrosinate hemoproteins.

39 r, host heme is sequestered in high-affinity hemoproteins.

40 bility of these mutants to utilize hemin and hemoproteins.

41 ce have the potential to interact with human hemoproteins.

42 ns, which scavenge heme bound iron from host hemoproteins.

43 vide guidelines for the rational design of b hemoproteins: a modular structure including a packed, st

44 In one model, the putative hemoprotein adopts different conformational states depen

45 l rich in hemoglobin and/or other CO-binding hemoproteins, also contained substantial CO concentratio

46 HO-2 is a hemoprotein and binds heme at heme regulatory motifs (HR

47 have been shown to affect proper assembly of hemoprotein and decrease activity of the mutants express

48 ound that P. serpens lacks most of the known hemoproteins and does not require heme for electron tran

49 Furthermore, during hyperoxia, lung hemoproteins and iron content were significantly increas

50 the catalytic boundaries of other oxidative hemoproteins and perform multiple functions.

51 Serratia marcescens, extracts heme from host hemoproteins and shuttles it to HasRSM, a specific hemop

52 revealing the ability of CO to bind to these hemoproteins and stimulate their binding at specific DNA

53 ein in heme binding and utilization of serum hemoproteins and the HmuR YRAP motif in serum hemoprotei

54 Diatomic ligands in hemoproteins and the way they bind to the active center

55 how the drug affects redox properties of the hemoprotein, and determined the 2.0 A X-ray structure of

56 ption, the formation of hemoglobin and other hemoproteins, and iron recycling in macrophages.

57 he out-of-plane distortions of porphyrins in hemoproteins are characterized by displacements along th

58 Hemoproteins are critical for the function and integrity

59 Oxygenated hemoproteins are known to react rapidly with nitric oxid

60 Hemoproteins are powerful oxidative catalysts.

61 Hemoproteins are ubiquitous in biology and are commonly

62 nes, hmuRSTUV, required for use of hemin and hemoproteins as iron sources.

63 Group A streptococci (GAS) can use heme and hemoproteins as sources of iron.

64 The heme of hemoproteins, as exemplified by horseradish peroxidase (

65 rotein with the characteristic Soret band of hemoprotein at 424 nm.

66 Hemoprotein-based scaffolds containing phosphorescent ru

67 sidues of HmuR that may be involved in hemin/hemoprotein binding and utilization, we constructed a se

68 rr generates H2O2 from O2 as found for other hemoproteins, but H2O2 is less effective in oxidizing th

69 sGC and is a member of a family of conserved hemoproteins, called the H-NOX family (Heme-Nitric Oxide

70 O-1, the first such intermediate observed in hemoprotein catalysis, completes our understanding of th

71 cDNAs in Escherichia coli, confirming their hemoprotein character.

72 At higher doses, nitrosyl hemoprotein complexes could also be detected in liver ti

73 detected as nitrosyl hemoglobin or nitrosyl hemoprotein complexes in rats was the result of the meta

74 of Escherichia coli is an iron-mineralizing hemoprotein composed of 24 identical subunits, each cont

75 from bovine and rat lung is a heterodimeric hemoprotein composed of alpha1 and beta1 subunits.

76 e guanylate cyclase (sGC) is a heterodimeric hemoprotein composed of alpha1 and beta1 subunits.

77 s a heterodimeric, nitric oxide (NO)-sensing hemoprotein composed of two subunits, alpha1 and beta1.

78 The nature of the [Fe(IV)-O] center in hemoprotein Compounds II has recently received considera

79 onal antibody raised against the recombinant hemoprotein confirmed primary expression of CYP2J2 prote

80 Another model proposes that the hemoprotein converts O2 to H2O2.

81 These findings with two monotopic ER hemoproteins, CYP2C11 and CYP3A4, and the polytopic ER p

82 tine in the active site of the monooxygenase hemoprotein cytochrome P450cam.

83 nt in each of the two major yeast CO-binding hemoproteins (cytochrome c oxidase and flavohemoglobin),

84 The transmembrane hemoprotein, cytochrome b(561) (b(561)), in the neuroend

85 agnetic resonance comparison of these ferric hemoproteins demonstrates that the mutation increases th

86 stantial extracellular heme is released from hemoproteins during hemorrhage and cell injury.

87 50s) are endoplasmic reticulum (ER)-anchored hemoproteins engaged in the metabolism of numerous xeno-

88 itric-oxide synthase, a cytochrome P450-like hemoprotein enzyme, catalyzes the synthesis of nitric ox

89 Cytochromes P450 (P450s) are hemoprotein enzymes committed to the metabolism of chemi

90 Cytoglobin is a hemoprotein expressed in response to oxidative stress in

91 In the presence of heme or hemoproteins, expression of the bhuRSTUV operon is induc

92 ctivity in COS-1 cells, and minor amounts of hemoprotein for this mutant were expressed in E. coli an

93 ssion increased the activity and quantity of hemoproteins found in several subcellular compartments,

94 and, in coral, by a 43-kDa catalase-related hemoprotein fused to the lipoxygenase that synthesizes t

95 Hemoproteins have been recognized for nearly a century a

96 Engineered hemoproteins have recently emerged as promising systems

97 e report that S. aureus can utilize the host hemoproteins hemoglobin and myoglobin, but not hemopexin

98 he concentration and/or activity of cellular hemoproteins (hemoglobin, catalase, and cytochrome c oxi

99 s efficient acquisition of Fe from hemin and hemoproteins (hemoglobin, myoglobin, and catalase).

100 As a hemoprotein, hemoglobin (Hb) can, in the presence of H(2

101 Hemoproteins, hemoglobin and myoglobin, once released fr

102 me-regulated eIF2alpha kinase (HRI) is a key hemoprotein in erythroid precursors that sense intracell

103 trate that cytoglobin is a stress-responsive hemoprotein in the hypoxia-induced hypertrophic myocardi

104 Cytochrome c is a multifunctional hemoprotein in the mitochondrial intermembrane space whe

105 in enhancing the catalytic efficiency of the hemoprotein in these reactions as well as modulating the

106 e tyrosine-liganded cAOS, a catalase-related hemoprotein in which a polyunsaturated fatty acid can en

107 heme can be transported and used in toto by hemoproteins in all six subcellular compartments examine

108 of the inflammatory response and binding to hemoproteins in order to restore homeostasis and sustain

109 Plant alpha-dioxygenases (PADOX) are hemoproteins in the myeloperoxidase family.

110 It is demonstrated with the purified hemoproteins in vitro that the terminal oxidase can outc

111 nstrate in vitro that acetaminophen inhibits hemoprotein-induced lipid peroxidation by reducing ferry

112 orms use dietary heme for incorporation into hemoproteins, ingested heme is also used as an iron sour

113 Myeloperoxidase (MPO), the phagocyte hemoprotein involved in neutrophil host defense and cons

114 st that the redox state of an oxygen-binding hemoprotein is involved in controlling the expression of

115 igh-spin iron(II) than in low-spin iron(III) hemoproteins is attributed to the much stronger correlat

116 The nature of Fe-O2 bonding in hemoproteins is debated for decades.

117 Soluble guanylate cyclase (sGC), a hemoprotein, is the primary nitric oxide (NO) receptor i

118 nding sites, similar to that which occurs in hemoproteins, is achieved so that monodentate ligands ad

119 These sensors incorporate cytochrome c', a hemoprotein known to bind nitric oxide selectively.

120 ivity and normal hepatic microsomal heme and hemoprotein levels, they had 20% and 13% of wild-type ac

121 ving the way to in vivo assembly of man-made hemoprotein maquettes and integration of artificial prot

122 PO and the novel mode of O(2) binding to the hemoprotein may provide important clues toward understan

123 e prooxidant effects of free iron, heme, and hemoproteins may be attributed to the formation of hyper

124 The hemoprotein-mediated oxidation of carboxylic acids, ubiq

125 ions for acetaminophen in diseases involving hemoprotein-mediated oxidative injury.

126 orm alpha-helices when incorporated in novel hemoprotein model compounds, peptide-sandwiched mesoheme

127 (II)-O(2) is relatively high, in contrast to hemoprotein model compounds.

128 Five alkyne-containing hemoprotein models have been synthesized in a convergent

129 peptides may influence the properties of the hemoprotein models.

130 radical-derived DMPO nitrone adducts in the hemoprotein Mycobacterium tuberculosis catalase-peroxida

131 The hemoprotein myoglobin is a model system for the study of

132 Cytochromes P450 are monotopic hemoproteins N-terminally anchored to the ER membrane wi

133 obacterium Nostoc commune UTEX 584 encodes a hemoprotein, named cyanoglobin, that has high oxygen aff

134 These motifs and the hemoprotein nature of HO-3 suggest a potential regulator

135 cess of coupled oxidation of model hemes and hemoproteins not involved in heme catabolism, the corres

136 en known for some years that the reaction of hemoproteins, notably cytochrome P450, with PN leads to

137 Neuroglobin is a highly conserved hemoprotein of uncertain physiological function that evo

138 Cytochrome P450s are hemoprotein oxygenases involved in natural product synth

139 ng subcellular-targeted, genetically encoded hemoprotein peroxidase reporters, that both extracellula

140 Hemoproteins play central roles in the formation and uti

141 The ubiquitous cytochrome P450 hemoproteins play important functional roles in the meta

142 and eosinophil peroxidase (EPO), a secreted hemoprotein, plays a central role in oxidant production

143 b Hemoproteins provide multiple examples of this behavior.

144 The catalase-related hemoprotein reacted rapidly and specifically with linole

145 e of exploring the scope of catalase-related hemoprotein reactivity toward fatty acid hydroperoxides,

146 The chlorite dismutase family of hemoproteins received its name due to the ability of the

147 We evaluate the streptococcal hemoprotein receptor (Shr), a conserved streptococcal pr

148 le guanylate cyclase (sGC) is a ferrous iron hemoprotein receptor for nitric oxide (NO).

149 d therefore was named Shr, for streptococcal hemoprotein receptor.

150 SiaA and Shr are the first hemoprotein receptors identified in S. pyogenes; their p

151 h DPI under 21% O(2) and then exposed to the hemoprotein reductant sodium dithionite (1 mmol/L) under

152 f Fe starvation and the presence of heme (or hemoproteins), regulates P(bhuR), a heme-responsive prom

153 kely to contribute to the reaction; and (iv) hemoprotein-rich tissues such as cardiac muscle are vuln

154 sinophil peroxidase (EPO), a highly cationic hemoprotein secreted by activation of eosinophils, is be

155 and that cytochrome c oxidase is likely the hemoprotein "sensor." Our findings also indicate that th

156 s the reduction of E. coli sulfite reductase hemoprotein (SiR-HP).

157 er of the Escherichia coli sulfite reductase hemoprotein (SiRHP) is exquisitely designed to catalyze

158 ed by the Escherichia coli sulfite reductase hemoprotein (SiRHP), we have determined crystallographic

159 ha subunit) and the other an iron-containing hemoprotein (SiRHP, the beta subunit), assemble to make

160 ogically relevant activator of the mammalian hemoprotein soluble guanylate cyclase (sGC).

161 a physiologically relevant activator of the hemoprotein soluble guanylate cyclase (sGC).

162 HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics.

163 The active site, found in the hemoprotein subunit (SiRHP), sits on the distal face of

164 te reductase shows a broad similarity to the hemoprotein subunit of sulfite reductase but has many si

165 rmediate succinyl CoA for incorporation into hemoproteins, such as the cytochromes needed for oxidati

166 here show that Gyc-88E from Drosophila is a hemoprotein that binds oxygen, as well as NO and CO.

167 e guanylate cyclase (sGC) is a heterodimeric hemoprotein that catalyzes the conversion of GTP to cGMP

168 oxide synthase (NOS) is a homodimeric flavo-hemoprotein that catalyzes the oxidation of L-arginine t

169 sGC is a heterodimeric hemoprotein that contains a Heme-Nitric oxide and OXygen

170 clase (sGC) is a nitric oxide- (NO-) sensing hemoprotein that has been found in eukaryotes from Droso

171 Aromatase, a cytochrome P450 hemoprotein that is responsible for estrogen biosynthesi

172 We also report a novel form of the hemoprotein that occurs in the absence of its cofactors.

173 Myeloperoxidase (MPO), a hemoprotein that uses H(2)O(2) as the electron acceptor

174 Nitric oxide synthases (NOS) are hemoproteins that catalyze the reaction of L-arginine to

175 e de novo, even though these animals contain hemoproteins that function in key biological processes.

176 ies similar to those of cytochrome P450-type hemoproteins that have undergone conversion to the catal

177 erfamily of genes encoding mostly microsomal hemoproteins that play a dominant role in the metabolism

178 c heme levels produces phenotypic changes in hemoproteins that protect cells from certain stresses.

179 In contrast to typical hemoproteins, the protein surface is not directly access

180 is typical for O(2) binding to other ferrous hemoproteins, the reaction involves several kinetically

181 mic factors that determine the assembly in b hemoproteins, the solution structure of the 98-residue p

182 ase (MPO) is an abundant mammalian phagocyte hemoprotein thought to primarily mediate host defense re

183 a strategy that expands the functionality of hemoproteins through orthogonal enzyme/heme pairs.

184 The ability of hemoproteins to catalyze epoxidation or hydroxylation re

185 urface proteins contribute to the binding of hemoproteins to S. pyogenes.

186 ialized cytochromes P450 or catalase-related hemoproteins transform fatty acid hydroperoxides to alle

187 and is required for utilizing hemin and all hemoproteins under iron-depleted conditions.

188 ococcus aureus scavenges heme-iron from host hemoproteins using iron-regulated surface determinant (I

189 In this study, we investigate hemoprotein utilization by S. pyogenes.

190 vium expresses, in addition to the BhuR heme/hemoprotein utilization system, an alternative RhuR-inde

191 emoproteins and the HmuR YRAP motif in serum hemoprotein utilization.

192 requirement by obtaining heme iron from host hemoproteins via IsdG- and IsdI-mediated heme degradatio

193 protein has revealed the first example of a hemoprotein which can utilize both sides of its heme (di

194 losoxidans cytochrome c', a mono-His ligated hemoprotein which reversibly binds NO and CO but not O(2

195 soluble form of guanylate cyclase (sGC) is a hemoprotein which serves as the only known receptor for

196 Heme is essential to the function of hemoproteins, which are involved in energy generation by

197 ctivation of the peroxynitrite anion (PN) by hemoproteins, which leads to its detoxification or, on t

198 ) was comparable to that observed with other hemoproteins whose activities are thought to be modulate

199 HRI is a hemoprotein with 2 distinct heme-binding domains.

200 ctra showed that TXAS was a typical low spin hemoprotein with a proximal thiolate ligand and had a ve

201 ells correlated with decreased expression of hemoprotein with a reduced difference spectrum of 450 nm

202 encoding a fusion protein of a catalase-like hemoprotein with an unusually short LOX (approximately 4

203 8R-lipoxygenase in Plexaura homomalla, is a hemoprotein with sequence similarity to catalases.

204 We found that HRI purified as a hemoprotein with the characteristic Soret band of hemopr

205 Coral allene oxide synthase (AOS), a hemoprotein with weak sequence homology to catalase, is

206 Hemoproteins with this type of engineered cofactor have