ライフサイエンスコーパス: heme protein

1 oding a cytochrome known as SHP (sphaeroides heme protein).

2 ed at or before significant nitrosylation of heme protein.

3 -iron complex formed by nitrosylation of non-heme protein.

4 m the unligated, pentacoordinate form of the heme protein.

5 e product was incorporated into a gas-sensor heme protein.

6 alytic potential of simple, de novo-designed heme proteins.

7 ons in the visible range, such as retinal or heme proteins.

8 as well as mechanisms of 5c-NO formation in heme proteins.

9 mics underlying the functional mechanisms of heme proteins.

10 atic landscape of the distal heme pockets of heme proteins.

11 ssible effects of strong hydrogen bonding in heme proteins.

12 ves their coordination to the iron center in heme proteins.

13 ars no significant homology with other known heme proteins.

14 on by deoxyhemoglobin, myoglobin, and tissue heme proteins.

15 4 is much slower than found for other ferric heme proteins.

16 n with deoxyhemoglobin and potentially other heme proteins.

17 the reactive energetics of Fe porphyrins and heme proteins.

18 ake, and good selectivity for NOS over other heme proteins.

19 dination encountered in bis-histidyl ligated heme proteins.

20 del for heme dynamics in myoglobin and other heme proteins.

21 drogen-bonding interactions with bound CO in heme proteins.

22 om dynamics in the biological functioning of heme proteins.

23 nge observed for diverse families of natural heme proteins.

24 or the isolation of functionally interesting heme proteins.

25 rved in the corresponding complexes of other heme proteins.

26 t precision in the design and engineering of heme proteins.

27 heme pocket structures of Hb, Mb, and other heme proteins.

28 urified P450s but not in heme alone or other heme proteins.

29 gradation of heme released from destabilized heme proteins.

30 rality of Trp-porphyrin electron transfer in heme proteins.

31 he accumulation/degradation of mitochondrial heme proteins.

32 osis lead to the leakage of large amounts of heme proteins.

33 key components of PCET/CPET active sites in heme proteins.

34 ing them collectively the CDE superfamily of heme proteins.

35 erved within functionally related classes of heme proteins.

36 nonspecific hydration of the active sites of heme proteins.

37 of reaction mechanisms of PN reactions with heme proteins.

38 r understand PN activation/detoxification by heme proteins, a definitive assignment of I435 is needed

39 myoglobin-like motif, display characteristic heme-protein absorption spectra, and bind oxygen reversi

40 Heme-proteins achieve differing functions through struct

41 hods allow us to determine the resilience of heme protein active sites.

42 the Fe atom in porphyrins designed to model heme protein active sites.

43 r-treated PGHS-1, producing iron chlorin and heme-protein adduct species.

44 tribution of bis-His coordination to ferrous heme protein affinity is limited, <3.0 kcal/mol.

45 The bacterial heme protein Alcaligenes xylosoxidans cytochrome c' (AXC

46 ns can be applied to tune E degrees of other heme proteins, allowing for comprehensive investigations

47 We examined iron nitrosylation of non-heme protein and enzymatic activity of the Fe-S cluster

48 mediates in the catalytic cycles of numerous heme proteins and a variety of model systems.

49 ctures, together with comparisons to ferrous heme proteins and an Fe(IV) oxene model.

50 correlation, including thiolate ligation in heme proteins and electron-donating meso-substituents in

51 in defining modes of oxygen binding in other heme proteins and enzymes.

52 l for investigating the chemistry of natural heme proteins and for designing artificial variants with

53 ted CYP3A4", as well as by a number of other heme proteins and hemin, suggesting that this is a heme-

54 what is found for spin-allowed NO binding to heme proteins and is several orders of magnitude larger

55 -based molecular devices and the function of heme proteins and methyl-coenzyme M reductase.

56 2.3, and 1.86, which are similar to those of heme proteins and model complexes with imidazole/thiolat

57 range of O2 activation processes mediated by heme proteins and model compounds with a focus on recent

58 facilitate future investigations of related heme proteins and model systems.

59 and structural investigations of HNO and RNO heme proteins and models.

60 Fe)(-)(CO)/nu(C)(-)(O) correlation curve for heme proteins and porphyrins with a proximal histidine o

61 nge of CO stretching frequencies observed in heme proteins and specific interactions observed in carb

62 Comparisons to copper and heme proteins and synthetic complexes are discussed.

63 nd distances from the heme iron in different heme proteins and the position of the distal histidine r

64 bin (Mb) is used as a model system for other heme proteins and the reactions they catalyze.

65 ant in understanding the association between heme-proteins and oxidative stress.

66 e-dependent growth, total heme, cytochromes, heme proteins, and iron levels).

67 a for bacterial bc(1) complex, other related heme proteins, and model compounds.

68 shed data on a range of other ligand-binding heme proteins, and support is given to the recent sugges

69 n other, more complex regulatory and sensing heme proteins, and the data are discussed in the context

70 al for virulence and disease, since heme and heme proteins are a major source of iron within the host

71 on-coupled electron transfer in two designed heme proteins are elucidated.

72 Heme proteins are extremely diverse, widespread, and ver

73 Several cysteinate-ligated heme proteins are known, but some fail to retain thiolat

74 The biological functions of heme proteins are linked to their rate and affinity cons

75 It is now well-established that mammalian heme proteins are reactive with various nitrogen oxide s

76 O proteins is a unique property because most heme proteins are readily autoreduced by excess NO and b

77 catalyzed by iron porphyrins and engineered heme proteins, as well as in the metabolism of various x

78 thesis that NikA is required for periplasmic heme protein assembly, the effects of a nikA mutation (n

79 heme from its sites of synthesis to sites of heme-protein assembly.

80 uettes allow the individual contributions of heme-protein association, iron-histidine ligation, and h

81 and thus preventing NO scavenging by ferric heme proteins at physiological NO concentrations.

82 Elucidating the inactivation pathways of heme protein-based carbene transfer catalysts should aid

83 Numerous heme proteins bind HNO, an important step for its biolog

84 Heme proteins bind the gaseous ligands XO (X = C, N, O)

85 to cytochrome c is not understood, and most heme proteins bind the prosthetic group by iron ion liga

86 establish that one function of the covalent heme-protein bonds in mammalian peroxidases is to protec

87 which we assign to the presence of covalent heme-protein bonds.

88 n of the bound CO in preventing poisoning of heme proteins by carbon monoxide.

89 litates refolding in these four-helix-bundle heme proteins by reducing the conformational freedom of

90 The separation of heme proteins by thiol-disulfide exchange chromatography

91 At basic pHs, the thiolate mini-heme protein can catalyze O(2) reduction when adsorbed o

92 The measured properties of the de novo heme proteins can be considered as a "default" range for

93 Following the recent discovery that heme proteins can catalyze the cyclopropanation of styre

94 synthases (NOSs, EC 1.14.13.39), a class of heme proteins capable of converting l-arginine to NO and

95 Hexacoordinate hemoglobins are heme proteins capable of reversible intramolecular coord

96 el for the active site in the six-coordinate heme protein, carbonmonoxy-myoglobin, are discussed in r

97 at lower frequencies than delta(FeCO) in all heme protein carbonyls reported to date, the results rep

98 Some bacterial heme proteins catalyze the coupling of two NO molecules

99 We have discovered that heme proteins catalyze the formation of organosilicon co

100 ndin H synthase-1 (PGHS-1) is a bifunctional heme protein catalyzing both a peroxidase reaction, in w

101 Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible stru

102 ially bound by the Tyr75 to form a high-spin heme-protein complex before slower coordination of the H

103 ligand shows only the rapid phase to form a heme-protein complex spectroscopically equivalent to tha

104 mimic the active sites of histidine-ligated heme proteins complexed with carbon monoxide.

105 Structural and functional details of heme protein complexes with HNO and the isoelectronic RN

106 GC variants might involve a weakening of the heme-protein contacts that are thought to be critical to

107 and analyzed to shed light on the nature of heme-protein contacts, other than that of the axial His,

108 The heme prosthetic group of heme proteins contains iron, which can be a limiting nut

109 The results are compared to heme proteins (CPO, P450(cam), HRP, Mb) where insertion

110 At acidic pH values heme-protein cross-linked myoglobin (Mb-H) forms as a pr

111 Although the mechanism of formation of heme-protein cross-linked myoglobin is thought to involv

112 kinetics of photoreduction of six different heme protein crystal species by X-ray radiation.

113 lograys already yields 50% ferrous iron in a heme protein crystal.

114 The membrane heme protein cytochrome b5 (b5) can enhance, inhibit, or

115 idate this approach with three variants of a heme protein cytochrome c (cyt c) and show that the meth

116 ortable oxidative stress sensor contains the heme protein cytochrome c (cyt c) as sensing element who

117 een demonstrated for the first time that the heme protein cytochrome c (Cyt c) can enter the interior

118 , interacts with the small electron transfer heme protein cytochrome c through both electrostatic and

119 trap in the folding-energy landscape of the heme protein cytochrome c.

120 Here, the heme protein, cytochrome b(562), is used to study the in

121 ve motions on a picosecond timescale for the heme protein, cytochrome c, as a function of oxidation a

122 ure-function relationships is presented: the Heme Protein Database (HPD).

123 Heme protein deficiencies were exacerbated in the iron-l

124 nism of hydroxylation of aromatic carbons by heme proteins, demonstrating that non-thiolate-ligated h

125 nding was studied in a collection of de novo heme proteins derived from combinatorial libraries of se

126 L-tryptophan oxidase flavoprotein and RebD a heme protein dimer with both catalase and chromopyrrolic

127 herol quinone (aTQ), and other constituents (hemes, proteins, DNA, and surfactant lipids).

128 For ferrous heme proteins, doming is associated with the respiratory

129 The data illustrate that heme protein E(m) values are modulated over a 300 mV ran

130 genes (ecdG,K) and one encoding a P450 type heme protein (ecdH).

131 in association, iron-histidine ligation, and heme-protein electrostatics to be elucidated.

132 minireview, selected monomeric and single b heme proteins endowed with distinct topological properti

133 The protein folding process of heme proteins entails generation of not only a correct g

134 roxidases (KatG) presents a new challenge in heme protein enzymology.

135 Topologically homologous four-helix-bundle heme proteins exhibit striking diversity in their refold

136 Myeloperoxidase, a heme protein expressed by select populations of artery w

137 Myoglobin is a monomeric heme protein expressed ubiquitously in skeletal and card

138 the slowest observed so far for this type of heme protein fold.

139 ndly alternative to sol-gels for stabilizing heme proteins for use as optical biosensors.

140 ression is mediated by heme availability for heme protein formation.

141 Nostoc sp. (Ns) H-NOX is a heme protein found in symbiotic cyanobacteria, which has

142 nonsymbiotic hemoglobins are hexacoordinate heme proteins found in all plants.

143 2/2Hbs are a class of single-domain heme proteins found in bacteria, ciliates, algae and pla

144 Truncated hemoglobins (trHbs) are heme proteins found in bacteria, plants, and unicellular

145 itrophorins (NPs) are a group of NO-carrying heme proteins found in the saliva of a blood-sucking ins

146 Cytochrome c' is a heme protein from a denitrifying variant of Rhodobacter

147 CooA, the CO-sensing heme protein from Rhodospirillum rubrum, regulates the e

148 CooA is a dimeric CO-sensing heme protein from Rhodospirillum rubrum.

149 pectra of the CO complexes for eight de novo heme proteins from two combinatorial libraries.

150 roles for heme distortion and NO bending in heme protein function are discussed.

151 Ligation by cysteine thiol in ferrous heme proteins has not been documented.

152 Multi-heme proteins have attracted much attention recently due

153 cades of research using the globins as model heme proteins have clearly highlighted the importance of

154 Many heme proteins have distal histidine residues that play i

155 ion, and electron transfer when bound to the heme proteins hemoglobin, myoglobin, cytochrome P450 and

156 lution viscosity at room temperature in four heme proteins: hemoglobin, myoglobin, a myoglobin mutant

157 Eosinophil peroxidase (EPO) is an abundant heme protein in eosinophils that catalyzes the formation

158 which encoded a putative plasma membrane di-heme protein in mouse duodenal mucosa.

159 an Escherichia coli four-helix bundle b-type heme protein in which the porphyrin prosthetic group is

160 he molecular interaction between nitrite and heme proteins in blood and tissues, the potential role o

161 nvolvement of surface-localized redox-active heme proteins in dissimilatory metal reduction.

162 opposite but intrinsically linked events, of heme proteins in mitochondria affect mitochondrial funct

163 equency (20-200 cm(-1)) vibrational modes of heme proteins in solution.

164 -vis) spectroelectrochemical measurements of heme proteins in the presence of a heme-bound fluoride i

165 vestigated the reactions of (*)NO with these heme proteins in their ferric resting form.

166 proteins or destabilization of intracellular heme proteins, increase intracellular levels of heme and

167 ue for the escape fraction relative to other heme proteins indicates the open nature of the heme pock

168 hese frequencies are typical of Fe-NO ferric heme proteins, indicating that the NP1 nitrosyl adduct h

169 fects of HO-1 against acute and chronic heme/heme protein-induced renal injury is summarized.

170 HO-1 is a critical protectant against acute heme protein-induced toxicity in vivo.

171 ence that this molecule acts as a marker for heme-protein-induced oxidative stress in vivo and may ex

172 ficant implications for the potential of the heme-protein interface to modulate the redox properties

173 n previously studied model complexes and the heme proteins is addressed; the difference appears to re

174 e nature of diatomic ligand recombination in heme proteins is elucidated by using a Landau-Zener mode

175 hat the intrinsic electroreactivity of these heme proteins is sufficient to account for physiological

176 d in Pseudomonas aeruginosa bacterioferritin heme protein, is described.

177 ng of cytochrome b(562), a four-helix-bundle heme protein, is hampered by heme dissociation.

178 l expression of holoMb, and presumably other heme proteins, is an ultra high fraction of folded, nati

179 s process by binding reversibly to RmFixL, a heme protein kinase whose deoxy form catalyzes the phosp

180 panel of methods that can be used to monitor heme protein kinetics, providing a rapid measurement tec

181 This is in contrast to other heme proteins known to have the His/Tyr axial ligand set

182 work in neuroglobin (Ngb), a hexacoordinated heme protein likely to be involved in neuroprotection, u

183 requirement for autocatalytic formation of a heme-protein link in P450 enzymes, but also show that ef

184 ults unambiguously demonstrate that a single heme-protein link is sufficient to protect the heme from

185 nctional roles played by the double covalent heme-protein linkage in cyt c, we have initiated a study

186 conformationally constrained double covalent heme-protein linkage, as exists in 1 and its parent prot

187 ra sulfur is sometimes incorporated into the heme-protein linkage.

188 ge conferred to cyt c by having two covalent heme-protein linkages rather than one: greater thermodyn

189 lectrochemistry were evaluated in a designed heme protein maquette.

190 Both heme protein maquettes chosen, heme b-[H10A24]2 and heme

191 lements of natural proteins into a family of heme protein maquettes, the lack of 3D structures, due p

192 sults identify a new way that cells regulate heme protein maturation during inflammation.

193 the synthesis of heme and its utilization in heme proteins; mechanisms underlying the toxicity of hem

194 terial periplasm or scavenges heme from host heme proteins, MmpL3 and MmpL11 are thought to transport

195 ll facilitate studies of HNO binding in many heme proteins, models, and related metalloproteins.

196 provide valuable insight into mechanisms for heme-protein modulation.

197 nhance electron flow also in the larger deca-heme proteins MtrC and MtrF, where heme-heme motifs with

198 idazole has been accomplished in a number of heme protein mutants, where it often serves to complemen

199 The heme protein myeloperoxidase (MPO) contributes criticall

200 ray of potentially damaging reactants by the heme protein myeloperoxidase.

201 For example, the ferrous heme protein myoglobin (Mb) has been shown to reduce nit

202 ncy on HO-1 in protecting against a specific heme protein, namely, hemoglobin: doses of hemoglobin wh

203 rdinate heme geometry similar to that of the heme protein neuroglobin.

204 o test the idea, expressly discussed for the heme protein nitrophorin, that porphyrin core distortion

205 n hydroxylated on the benzylic carbon by the heme protein NovI, generating beta-OH-Tyr-S-NovH.

206 ut substrate, is represented by the low-spin heme protein only, while the slow-reducible fraction is

207 ic processes, such as renal incorporation of heme proteins or destabilization of intracellular heme p

208 These data indicate that the activity of the heme protein peroxidase was enhanced by NO, whereas tyro

209 and pods, which clearly suggests that these heme proteins play additional roles unrelated to nitroge

210 Heme proteins play essential roles in biology, but littl

211 alent nature of the porphyrin environment in heme proteins precludes using many spectroscopic approac

212 lobins (nsHbs) are a class of hexacoordinate heme proteins present in all plants.

213 Globins are oxygen-binding heme proteins present in bacteria, protists, fungi, plan

214 ward understanding the molecular function of heme proteins; present methods, however, have not proven

215 Activation of myeloperoxidase (MPO), a heme protein primarily expressed in granules of neutroph

216 teins bind heme.(2) This collection of novel heme proteins provides a unique opportunity for an unbia

217 tern is common to a wide diversity of ferric heme proteins, raising the question of the biological re

218 ues that play important roles in determining heme protein reactivity.

219 fold, heme type and heme axial ligands, with heme protein reduction potential values in a web-searcha

220 Thus, the 1 V range observed in heme protein reduction potential values in biological sy

221 ividual heme proteins which demonstrate that heme protein reduction potential values, E(m), span the

222 hown that myeloperoxidase (MPO), an abundant heme protein released by activated leukocytes, can oxidi

223 emAT from Bacillus subtilis is a new type of heme protein responsible for sensing oxygen.

224 he heme maquettes and other de novo designed heme proteins reveals global trends in the E(m) values o

225 pectroscopy is applied to a series of ferric heme protein samples.

226 n electrostatic response from these designed heme protein scaffolds.

227 ontributes to the diverse functions of other heme protein scaffolds.

228 Myeloperoxidase (MPO), a heme protein secreted by activated leukocytes, generates

229 Myeloperoxidase, a heme protein secreted by activated phagocytes, is a pote

230 s contain LDL oxidized by myeloperoxidase, a heme protein secreted by activated phagocytes.

231 Myeloperoxidase, a heme protein secreted by neutrophils, monocytes, and mac

232 (HOCl) produced by myeloperoxidase (MPO), a heme protein secreted by phagocytes.

233 Investigated mutations of the heme protein seemed to have no significant impact on N-r

234 Here, we identify a heme protein sensor (SONO) that displays femtomolar affi

235 ts, by analogy with earlier studies of other heme proteins, several bands associated with modes attri

236 ed functions of exchangeable/labile heme and heme proteins should be of interest to biological chemis

237 ith membrane heme proteins whereas cytosolic heme proteins signal the redox state, releasing modulato

238 ll, the CO binding properties of the de novo heme proteins span a narrow range of values near the cen

239 HemO forms a 1:1 complex with heme and has a heme protein spectrum similar to that previously reporte

240 parative mutagenesis can be used to increase heme protein stability and improve expression yields in

241 tants that define electron flow in the tetra-heme protein STC by combining a novel projector-operator

242 database is the first of its kind to combine heme protein structural classifications including protei

243 global analysis, a new web-based resource of heme protein structure-function relationships is present

244 st to predict/refine elements of diamagnetic heme protein structures.

245 e is the reduction of the ferrous oxygenated heme protein, subsequent reaction intermediates do not n

246 that is reduced in the absence of oxygen by heme proteins such as CYP450 enzymes.

247 de derivatives of several well characterized heme proteins such as cytochrome c peroxidase, horseradi

248 riety of proteins including thiolate-ligated heme proteins such as cytochrome P450 2B1 and PGI2 synth

249 y be mediated by its reactivity with ferrous heme proteins such as myoglobin and hemoglobin.

250 he dissociation rate of O2 relative to other heme proteins such as myoglobin.

251 ormational energetics of ligand switching in heme proteins such as those observed in nitrite reductas

252 ed our understanding of various functions of heme proteins, such as O2 storage and transport, degrada

253 th S = 5/2 or 1/2 are models for a number of heme protein systems, including cytochromes c'.

254 a carbon monoxide- (CO-) sensing homodimeric heme protein that activates the transcription of genes r

255 peroxidase (DHP) from Amphitrite ornata is a heme protein that can function both as a hemoglobin and

256 Human cystathionine beta-synthase is a heme protein that catalyzes the condensation of serine a

257 thionine beta-synthase (CBS) is a tetrameric heme protein that catalyzes the PLP-dependent condensati

258 ) and overexpressed myeloperoxidase (MPO), a heme protein that converts hydrogen peroxide to hypochlo

259 om Desulfovibrio vulgaris is a small helical heme protein that displays apparent two-state equilibriu

260 MPO is an abundant neutrophil-derived heme protein that is part of the antimicrobial defense s

261 n (Ngb) is a newly discovered oxygen-binding heme protein that is primarily expressed in the brain of

262 Nitrophorin 4 (NP4) is a heme protein that stores and delivers nitric oxide (NO)

263 talase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxid

264 ptophan dioxygenase (hTDO) are two important heme proteins that degrade the essential amino acid, l-t

265 Catalases are heme proteins that detoxify H(2)O(2), and many bacteria

266 proteins, and that ferric cysteinate-ligated heme proteins that fail to retain such ligation on reduc

267 sessment of the functional potentialities of heme proteins that have not been prejudiced either by ex

268 Nitrophorins are ferric heme proteins that transport nitric oxide (NO) from bloo

269 rstand the mechanism of radical formation on heme proteins, the formation of radicals on hemoglobin w

270 on to this ubiquitous family of metabolizing heme proteins, the pathway from the twice reduced dioxyg

271 In addition to these prototypical heme proteins, there are emergent, critical roles of exc

272 el system for the study of ligand binding to heme proteins; this investigation affords the first stru

273 To assess the capabilities of the de novo heme proteins to bind diatomic ligands, we measured the

274 tion with deoxygenated hemoglobin and tissue heme proteins to form NO.

275 sect Rhodnius prolixus uses nitrophorin 4, a heme protein, to deliver nitric oxide (NO) to a victim,

276 ensable response in protecting against acute heme protein toxicity in vivo.

277 In the glycerol model of heme protein toxicity-one characterized by myolysis, hem

278 CooA is a CO-dependent heme protein transcription factor of the bacterium Rhodo

279 Heme proteins utilize the heme cofactor, an iron porphyr

280 Iron nitrosylation of non-heme protein was coincidental with decreases in the nonn

281 Cytochrome P450 heme protein was detected at a concentration of 44.6 pic

282 al accumulation of heme oxygenase-1, another heme protein, was also regulated by oxygen level and Lon

283 structure/function relationships of this new heme protein, we have used resonance Raman spectroscopy

284 iron(IV)hydroxide pK(a) of histidine ligated heme proteins, we have probed the active site of myoglob

285 re, we show that in contrast to other c-type heme proteins, where misligations in the unfolded states

286 tion potentials in association with membrane heme proteins whereas cytosolic heme proteins signal the

287 control the geminate recombination of CO in heme proteins, whereas spin selection rules play a minor

288 nd functional characterization of individual heme proteins which demonstrate that heme protein reduct

289 Dioxygenases (NODs), microbial and mammalian heme proteins which facilitate *NO detoxification/homeos

290 MauG is a novel 42 kDa di-heme protein, which is required for the biosynthesis of

291 been proposed that cells sense hypoxia by a heme protein, which transmits a signal that activates th

292 Heme proteins, which reversibly bind oxygen and display

293 ng cytochrome c (M) (CytM), a cryptic c-type heme protein widespread in cyanobacteria.

294 e first report of verdoheme generated from a heme protein with exclusive methionine ligation to the h

295 omains are a conserved family of gas-sensing heme proteins with a divergent fold that are critical to

296 to those of the nu3 and nu2 bands of c-type heme proteins with bis-histidine coordination.

297 both diamagnetic (CO) and paramagnetic (NO) heme proteins with in both cases the metal-ligand bindin

298 sent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity

299 Cytochromes c' are pentacoordinate heme proteins with sterically hindered distal sites that

300 terature on Ru- and Fe porphyrins (including heme proteins) with sulfur-containing ligands or substra

301 iols, N-nitros-amines, and iron-nitrosylated heme proteins within 1-30 minutes of reperfusion.