ライフサイエンスコーパス: heme

1 eld the parasite from the harmful effects of heme.

2 errini and Paragonimus westermani, also bind heme.

3 ly higher peroxidase activity than Abeta(40)-heme.

4 ev-erbbeta ineffective as a sensor of Fe(3+)-heme.

5 erred to mitochondria for incorporation into heme.

6 mpounds, such as fatty acids, bilirubin, and heme.

7 tive electron transfer (ET) pathway from the heme.

8 inding form of hemoglobin that readily loses heme.

9 nd intermonomer Coulombic effects between bL hemes.

10 N-based nucleophiles on synthetic ferric-NO hemes.

11 STC in the thermodynamic downhill direction (heme 1-->4) is approximately 3 x 10(6) s(-1).

12 o-catalytically forms an ester bond with the heme 5-methyl, and the immobilized Glu-310 contributes t

13 Moreover, the heme 7-propionate is positioned in the active site and p

14 OX relies on its redox-active metal centers (heme a and a3, CuA and CuB) to reduce oxygen and pump pr

15 5 appears to be important for the process of heme a biosynthesis and transfer to maturing CcO.

16 he electric dipole moment of residues around heme a changes with the redox state, hence suggesting th

17 Ser382 and the hydroxyethylfarnesyl group of heme a In fact, the region around His413 only became suf

18 Heme a is an essential metalloporphyrin cofactor of the

19 s concluded that Pet117 mediates coupling of heme a synthesis to the CcO assembly process in eukaryot

20 port proton transfer from the N phase toward heme a via neutral His413, regardless of a labile H bond

21 SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of approxima

22 on these results we propose a mechanism for heme acquisition by HmuUV-T where the substrate-loaded S

23 Finally, we demonstrate that heme activates DGCR8 to recognize pri-miRs by specifical

24 First, the heme active site binds carbon monoxide in both micelles

25 micelles and fibers, demonstrating that the heme active site in both morphologies is accessible to s

26 ively blocked in hem1Delta mutant cells, the heme analog zinc mesoporphyrin IX (ZnMP) first accumulat

27 CCS), leading to two thioether bonds between heme and a conserved CXXCH motif of cyt c In cyt c, hist

28 -erbbeta HRM in regulating interactions with heme and NCoR1 and advance our understanding of how sign

29 ntly, successive addition of heme as well as heme and NO to purified recombinant apo-DnrF protein inc

30 ecular-weight complexes when associated with heme and that these complexes are reorganized by a stack

31 ent ineffective erythropoiesis, highlighting heme and translation in the regulation of erythropoiesis

32 lso inhibits the peroxidase-like activity of heme, and (ii) MF6p/HDMs from other trematodes, such as

33 in slower proliferation, decreased cellular heme, and marked changes in cellular morphology so that

34 Most importantly, successive addition of heme as well as heme and NO to purified recombinant apo-

35 Unpaired globin chains, with heme attached to them, accumulate in thalassemic erythro

36 Since Enterococcus faecalis is a natural heme auxotroph and cause of bloodstream infection, we ex

37 Supplementation of the culture medium of the heme-auxotrophic SCV with heme, but not iron, restored g

38 balance globin synthesis with the amount of heme available for hemoglobin production.

39 coproheme III as substrate and cofactor, and heme b as the product.

40 m bacteria, is required for the insertion of heme b into respiratory chain enzymes.

41 ase activity, indicating that the cofactors (hemes b and copper for CcoN and cytochromes c for CcoO a

42 tions to incorporate the biological cofactor heme-B for catalysis.

43 results indicate that the iron released from heme because of HO activity contributes to the pathophys

44 and mapped the protein regions required for heme binding and for other biological functions.

45 insight into the role of protein dynamics in heme binding and release in bacterial heme transport pro

46 ructural rearrangement and protection of the heme binding pocket.

47 al rearrangement of the C-terminal domain of heme binding protein (PhuS) is required for interaction

48 nd biochemical approaches, we identified two heme binding sites and a hemoglobin binding site in PfHD

49 visible and EPR spectroscopy to characterize heme binding to DnrF and subsequent NO coordination.

50 In this study, we dissected the kinetics of heme binding to Rev-erbbeta and provided a Kd for Fe(3+)

51 Heme binding to Rev-erbbeta indirectly facilitates its i

52 r that undergoes fluorescence quenching upon heme binding.

53 W-catalyzed heme transfer but not for stable heme binding.

54 revealed that specific modifications in the heme-binding (R374W and R448C) or substrate-binding (W11

55 lytic flavin adenine dinucleotide (FAD)- and heme-binding domains of Cylindrospermum stagnale NOX5.

56 iron, which is poised for transfer into the heme-binding pocket of IsdB.

57 te via a hydrophobic channel adjacent to the heme-binding pocket.

58 a hepatica that belongs to a broad family of heme-binding proteins (MF6p/helminth defense molecules (

59 We also demonstrated that (i) the heme-binding region is located in the MF6p/FhHDM-1 C-ter

60 ween the Cys residues at the apocytochrome c heme-binding site (CXXCH).

61 e more than one modification, cluster in the heme-binding site, supporting a hierarchy of vulnerable

62 Fe(3+)-heme binds in a 6-coordinate complex with axial His and

63 yield quantitative insights into fundamental heme biology.

64 e mitochondrial AAA+ unfoldase ClpX promotes heme biosynthesis by activation of delta-aminolevulinate

65 A1 transcriptional target, AKAP10, regulates heme biosynthesis during erythropoiesis at the outer mit

66 istinctive differences, with upregulation of heme biosynthesis genes prominently in RP-mediated DBA a

67 elopment and sheds new light on tetrapyrrole/heme biosynthesis in plant mitochondria.

68 results in pathological accumulation of the heme biosynthesis intermediate protoporphyrin IX (PPIX).

69 When heme biosynthesis is selectively blocked in hem1Delta mu

70 Because the heme biosynthesis pathway is highly conserved in eukaryo

71 ia (EPP) is a rare inherited disorder of the heme biosynthesis pathway resulting in the accumulation

72 The heme biosynthesis pathway was particularly amenable to i

73 ed that Gram-positive pathogens use a unique heme biosynthesis pathway, which implicates this pathway

74 report the identification of a new mutant in heme biosynthesis, hem13-1, that is hypersensitive to HU

75 aches to demonstrate that tellurite inhibits heme biosynthesis, leading to the accumulation of interm

76 m-positive bacteria, an enzyme essential for heme biosynthesis.

77 th the direct phosphorylation of the crucial heme biosynthetic enzyme, ferrochelatase (FECH) by prote

78 in the activity of a specific enzyme in the heme biosynthetic pathway.

79 orate intramonomer Coulombic effects between hemes bL and bH and intermonomer Coulombic effects betwe

80 ture medium of the heme-auxotrophic SCV with heme, but not iron, restored growth, hemolysin and staph

81 ) mice treated with SnPP exhibited decreased heme catabolism and diminished iron release as well as r

82 Heme catabolism exerts physiological functions that impa

83 Therefore, new therapies that suppress heme catabolism may be beneficial in ameliorating the an

84 This was supported by an altered heme catabolism, indirectly reflecting in elevated uncon

85 phyrin cofactor (Ir(Me)-PIX) in place of the heme catalyze enantioselective intramolecular C-H bond a

86 in ferric sulfide, the first intermediate in heme-catalyzed sulfide oxidation.

87 tological and in vivo MRI assessments of non-heme cellular iron revealed that preclinical prostate tu

88 e radical SAM protein family HemW/RSAD1 is a heme chaperone catalyzing the insertion of heme into hem

89 e, we report that a radical SAM protein, the heme chaperone HemW from bacteria, is required for the i

90 ar interest are radical SAM enzymes, such as heme chaperones, that insert heme into respiratory enzym

91 Heme proteins utilize the heme cofactor, an iron porphyrin, to perform a diverse r

92 itochondria, possesses a covalently attached heme cofactor.

93 DnrF detects NO via its bound heme cofactor.

94 Proteins carrying an iron-porphyrin (heme) cofactor are essential for biological O2 managemen

95 compared to horseradish peroxidase, the ten heme cofactors enable excellent electronic communication

96 based on a weak Kd value for the Rev-erbbeta.heme complex of 2 mum determined with isothermal titrati

97 O2 binding to the Fe(II) heme complex of its N-terminal globin domain strongly st

98 of view the peroxidase activity of the Abeta-heme complex seemed quite attractive to pursue this goal

99 observed to coordinate heme iron in an IsdB.heme complex structure.

100 ing for an assay system that can be used for heme concentration determination.

101 crease the readout even in the case of a low heme concentration is favorable.

102 rythroid precursors that sense intracellular heme concentrations to balance globin synthesis with the

103 Cyt c, a heme containing metalloprotein is located in the interme

104 It lacks all genes encoding heme-containing cytochrome P450 proteins.

105 ng catalytic intermediates common to natural heme-containing enzymes.Catalytic mechanisms of enzymes

106 ng micelles yet was significantly reduced in heme-containing fibers.

107 matics as a member of the FRD superfamily of heme-containing membrane proteins, which include the NAD

108 Second, peroxidase activity was observed in heme-containing micelles yet was significantly reduced i

109 ive intermediates has come from the study of heme-containing proteins and related metalloporphyrin co

110 found that an inhibitor of flavoproteins and heme-containing proteins, diphenyleneiodonium, effective

111 L mutations severely compromise activity and heme content, although alkene products are formed from s

112 nheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the

113 ing oxygen reductase that is a member of the heme-copper superfamily that utilizes ubiquinol-8 (Q8H2)

114 ociation upon reduction of Fe(3+)- to Fe(2+)-heme, decreased binding affinity by >20-fold.

115 HRI is activated by heme deficiency and oxidative stress, and it phosphoryla

116 The mutation is hypomorphic and causes heme deficiency, which likely sensitizes the cells to th

117 h the presence of intraplaque hemorrhage and heme degradation products, particularly bilirubin by usi

118 A heme-dependent conformational rearrangement of the C-ter

119 KatG is a bifunctional, heme-dependent enzyme in the front-line defense of numer

120 We previously uncovered a heme-dependent metabolic switch for transient induction

121 osed to preferentially stimulate oxidized or heme-depleted, but not native sGC.

122 bound to HemW was actively transferred to a heme-depleted, catalytically inactive nitrate reductase,

123 Heme deprivation in the tsetse fly anterior midgut might

124 s of bacterial phytochromes (BphPs) utilizes heme-derived biliverdin tetrapyrrole, which is ubiquitou

125 Here, we characterize heme detoxification protein, PfHDP, a major protein invo

126 e that Rv2633c is the first example of a non-heme di-iron catalase, and conclude that it is a member

127 e alpha subunits of Hb are refolded with the heme displaced to the interface with IsdB.

128 ysis, we localized drug binding to the beta1 heme domain of sGC proteins from the hawkmoth Manduca se

129 ocalization of stimulator binding to the sGC heme domain reported here resolves the longstanding ques

130 rved cleft between two subdomains in the sGC heme domain.

131 olution of the distribution toward increased heme doming and larger enthalpic barriers.

132 arriers associated with heterogeneity in the heme doming conformation.

133 nless quantum mechanical tunneling along the heme doming coordinate is also included as an active cha

134 l fluids that resist oxidative damage during heme-driven inflammation.

135 ow kinetic measurements show that increasing heme E degrees ' by ca. 210 mV results in increases in e

136 models to investigate the mechanism by which heme E degrees ' modulates oxidase activity.

137 re preserves access to the diverse chemistry heme enables, while minimizing cellular damage caused by

138 dence that axial ligands are changed and the heme environment is altered.

139 Myeloperoxidase, a heme enzyme released by polymorphonuclear neutrophils, a

140 n fatty acyl-CoA reductase 1 in complex with heme exhibited a significantly higher peroxidase activit

141 terized an alpha-ketoglutarate-dependent non-heme Fe(II) dioxygenase that forged the azetidine ring o

142 able of shifting this equilibrium toward the heme-free apo-sGC species.

143 ween 20 showed that cinaciguat activates the heme-free enzyme in a concentration-dependent manner wit

144 Assuming a sensitive balance between heme-free, ferric, and nitric oxide-sensitive ferrous sG

145 pathogen Staphylococcus aureus that extracts heme from hemoglobin (Hb) to enable growth on Hb as a so

146 ce signaling and transport systems to obtain heme from the host.

147 3 participates in the mobilization of stored heme from the vacuole to the cytosol.

148 uple, and we demonstrate that the prosthetic heme group is post-translationally modified and cross-li

149 le CIU revealed the protective effect of the heme group on the structure of CYP142A1.

150 ate constants for ET between the constituent heme groups, have so far evaded experimental determinati

151 for further transfer to internal or external heme groups.

152 gas binding site on the proximal side of the heme has also been characterized, using xenon pressure o

153 Labile heme has been suggested to have an impact in several sev

154 ease (AD), however, decreased levels of free heme have been reported.

155 rger deca-heme proteins MtrC and MtrF, where heme-heme motifs with sub-optimal edge-to-edge distances

156 Here we report the set of heme-heme theoretical ET rate constants that define elec

157 hat bound the modeled PfHDP structure in the heme/hemoglobin-binding pockets from Maybridge Screening

158 This protection is sustained by heme-hemopexin complexes in biological fluids that resis

159 n conditions to control the synthesis of non-heme high-valent mu-oxo and mu-hydroxo Mn species from M

160 MF6p/HDMs are of interest for understanding heme homeostasis in trematodes and as potential targets

161 interaction between the Yersinia pestis ABC heme importer (HmuUV) and its partner substrate-binding

162 H2S reactivity of the coordinately saturated heme in neuroglobin is expected a priori to be substanti

163 is known to bind heme, the molecular role of heme in pri-miR processing is unknown.

164 indings suggest that MF6p/HDMs can transport heme in trematodes and thereby shield the parasite from

165 , CO-inhibited (carboxy), and O2-bound (oxy) hemes in myoglobin (MB) and hemoglobin (HB) solutions an

166 CLPX has also been reported to mediate heme-induced turnover of ALAS.

167 her than changing the oligomerization state, heme induces a conformational change in DGCR8.

168 We found that heme induces transcription of HAP4, the transcriptional

169 evious findings on the mechanism of MF6p/HDM-heme interactions and mapped the protein regions require

170 ctivity and less accumulation of off-pathway heme intermediates.

171 a heme chaperone catalyzing the insertion of heme into hemoproteins.

172 nzymes, such as heme chaperones, that insert heme into respiratory enzymes.

173 This enzyme is essential for processing heme into the electron transport chain for use as an ele

174 nt implications on electronic charge of both heme iron and O2 , resulting in increased O2 dissociatio

175 ing function by modulating bonding between a heme iron and the sulfur in a methionine residue.

176 (His19) of CXXCH acts as an axial ligand to heme iron and upon release of holocytochrome c from HCCS

177 itors described so far, does not bind to the heme iron atom and has a novel binding mode.

178 lu, suggest that water displacement from the heme iron can be affected in activator-bound CYP46A1.

179 Natural fusions between the non-heme iron containing PDO and rhodanese, a thiol sulfurtr

180 duction and in regulating protein stability, heme iron coordination, and spin state.

181 Prolyl-4-hydroxylase (P4H) is a non-heme iron hydroxylase that regio- and stereospecifically

182 viously, Tyr(440) was observed to coordinate heme iron in an IsdB.heme complex structure.

183 Although the absorption of heme iron is poorly understood, nonheme iron is transpor

184 Renal non-heme iron levels were increased in the (New Zealand Blac

185 er from Hb that involves unfolding of Hb and heme iron ligand exchange.

186 To investigate the extent of endogenous heme iron nitrosylation an experimental in vitro model t

187 e iron, the basic mechanism(s) governing sGC heme iron recycling to its NO-sensitive, reduced state r

188 dergoes only minor substrate binding-induced heme iron spin state shift toward high spin by compariso

189 Heme iron was associated with a higher risk of T2D even

190 as evaluated in the reaction of nitrite with heme iron, and the observed rate constants of the reacti

191 After additional adjustment for heme iron, only red meat intake remained significantly a

192 oxygen species are known to oxidize the sGC heme iron, the basic mechanism(s) governing sGC heme iro

193 lular iron-storage protein ferritin, and for heme iron, the chaperone proteins haptoglobin and hemope

194 8) and His(89) of alphaHb, coordinate to the heme iron, which is poised for transfer into the heme-bi

195 by permanent displacement of Met80 from the heme iron.

196 gaseous ligands through coordination to the heme iron.

197 dence for this site being used to access the heme iron.

198 ron, which has lower absorption than that of heme iron.We assessed the efficacy of the consumption of

199 using tin protoporphyrin IX (SnPP) decreased heme-iron recycling in the liver and ameliorated anemia

200 Quantitative analysis of labile heme is of fundamental importance to understanding how n

201 Heme is ubiquitous, yet relatively little is known about

202 t is at least partly due to the low cellular heme level.

203 ciparum, we have quantified cytosolic labile heme levels in intact, blood-stage parasites.

204 findings, we postulate that T. brucei senses heme levels via the flagellar TbHrg protein.

205 des mechanistic insights into how the distal heme ligand in neuroglobin caps its reactivity toward H2

206 tation assay, substitution of the His or Cys heme ligands in Rev-erbbeta was accompanied by a signifi

207 educes this disulfide bond to allow covalent heme ligation.

208 ons among the apocytochrome c, CcmG, and the heme-ligation components CcmF, CcmH, and CcmI.

209 RNAi-induced down-regulation of TbHrg in heme-limited culture conditions resulted in slower proli

210 ced factor 1alpha (HIF-1alpha) and increased heme-mediated protein degradation.

211 th post-translational mechanisms to regulate heme metabolism during normal development.

212 e multiple mechanisms by which CLPX controls heme metabolism.

213 ctors (NADPH, FAD, and two membrane-embedded heme moieties) injects electrons from the intracellular

214 ficient cytosolic electron donor to the MsrQ heme moieties.

215 to [Fe4S4](2+) clusters and low-spin Fe(II) hemes, most of which were associated with mitochondrial

216 le, namely the phenyl anion, with the ferric heme nitrosyl [(OEP)Fe(NO)(5-MeIm)](+) generates a mixtu

217 me nonheme site and confer HCO activity in a heme-nonheme biosynthetic model in myoglobin.

218 due to the direct electron exchange between heme of ADH and modified AuNPs.

219 to Rev-erbbeta and provided a Kd for Fe(3+)-heme of approximately 0.1 nm Loss of the HRM axial thiol

220 s in the low nanomolar range, and the Fe(3+)-heme off-rate is on the order of 10(-6) s(-1) making Rev

221 ired for interaction with the iron-regulated heme oxygenase (HemO).

222 s that interact with HIV-1 MA, we found that heme oxygenase (HO-2) specifically binds the myristate m

223 To assess intracellular heme oxygenase 1 (HO-1) isolated PBMCs were used.

224 kers (matrix metalloproteinase 1 [MMP-1] and heme oxygenase 1 [HO-1]), and proinflammatory cytokines

225 tional downregulation of the redox regulator heme oxygenase-1 (HO-1 or HMOX1).

226 f2, NAD(P)H quinone oxidoreductase 1 (NQO1), heme oxygenase-1 (HO-1) and a high ratio of Bcl-2/Bax.

227 Heme oxygenase-1 (HO-1) is a stress-inducible, anti-infl

228 overexpression of the cytoprotective enzyme heme oxygenase-1 (HO-1) play a critical role in the grow

229 Heme oxygenase-1 (HO-1) protein is an antioxidant enzyme

230 ter antioxidant transcription factor, and of heme oxygenase-1 (HO-1), one of its main target genes, i

231 Heme oxygenase-1 (HO-1, Hmox1) regulates viability, prol

232 via Nrf2 pathway, enhancing GSH/GSSG ratio, heme oxygenase-1 and glyoxalase 1 in liver tissue.

233 duced expression of the Nrf2 target protein, heme oxygenase-1 in the skin and protected against UVB-i

234 ntioxidant systems such as peroxiredoxins-1, heme oxygenase-1, and anti-apoptotic factors, including

235 e regulation of key Nrf2 target genes (i.e., heme oxygenase-1, NAD(P)H dehydrogenase, quinone 1, glut

236 Here, we report that mice deficient in heme oxygenase-2 (HO-2), which generates the gaseous mol

237 ate binding site within the cellular protein heme oxygenase-2 that acts as a trap to inhibit N-myrist

238 ncreased inducible nitric oxide synthase and heme-oxygenase 1 expression, and increased MDA and plasm

239 ncreased inducible nitric oxide synthase and heme-oxygenase 1 expression, and increased plasma creati

240 the CX3CR1 receptor induced upregulation of heme-oxygenase-1 (HMOX-1), an antioxidant and anti-infla

241 lph is a new allele of HEME OXYGENASE1 (HY1) that encodes the key protein in th

242 ing an [4Fe-4S] cluster, and we observed one heme per subunit of HemW.

243 that the dimeric DnrF bound one molecule of heme per subunit.

244 table, monomeric, glycosylated, and secreted heme peroxidase with homology to mammalian peroxidases.

245 analysis, a hybrid type A member of class I heme peroxidases [TcAPx-cytochrome c peroxidase (CcP)],

246 f the oxidation of uric acid by inflammatory heme peroxidases.

247 e and comparative reactivity of two low-spin heme-peroxo-Cu complexes, LS-4DCHIm, [(DCHIm)F8Fe(III)-(

248 te sterics, partially mediated by an unusual heme-polypeptide ester bond.

249 Our findings indicate that a labile heme pool ( approximately 1.6 microM) is stably maintain

250 Furthermore, we show that the heme precursor 5-aminolevulinic acid, which is used as a

251 antially lower than that of the 5-coordinate hemes present in myoglobin and hemoglobin.

252 he reversible oxidation and reduction of ADH heme proceeded at around -0.05V vs. SCE.

253 Although heme production is critical for many cellular processes,

254 ges with the binding of dioxygen (O2) to the heme prosthetic groups of the globin chains: from parama

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

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

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

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

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

260 Multi-heme proteins have attracted much attention recently due

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

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

263 Heme proteins utilize the heme cofactor, an iron porphyr

264 tive and inactive forms were observed on the heme-proximal side (helix H5), at the dimerization inter

265 aling striking structural differences on the heme-proximal side of the globin domain.

266 sults suggest that structural changes at the heme-proximal side, the globin domain-dimerization inter

267 Combining UV-visible spectroscopy, heme quantification, and site-directed mutagenesis of hi

268 While heme reduction potential (E degrees ') of different HCO

269 , yet molecular mechanisms by which iron and heme regulate erythropoiesis are not completely understo

270 Heme-regulated eIF2alpha kinase (HRI) is a key hemoprote

271 pTRS1 bound an additional eIF2alpha kinase, heme-regulated inhibitor (HRI), and inhibited eIF2alpha

272 is and Cys ligands, the latter provided by a heme-regulatory motif (HRM).

273 witch from His-209 to His-212 and triggering heme release to HemO.

274 Circulating hemoglobin and heme represent erythrocytic danger-associated molecular

275 ctrum is compared with a spectrum in buffer, heme-resonance bands are absent, indicating loss of Met-

276 Rev-erbbeta is a heme-responsive transcription factor that regulates gene

277 d non-Abeta-derived peptides in complex with heme revealed that the peroxidase-like activity signific

278 summarize the structure and function of the heme-sensing and transport systems of pathogenic bacteri

279 Rev-erbbeta was thought to be a heme sensor based on a weak Kd value for the Rev-erbbeta

280 cal and spectral features revealed analogous heme sites in MB and HB and the absence of low-spin (LS)

281 , a large internal cavity is involved in the heme sliding mechanism to achieve binding of gaseous lig

282 nds that induce substrate-like shifts in the heme spectrum of CYP126A1.

283 itantly with the accumulation of ferryl-like heme states.

284 Increased heme synthesis, even under conditions of glucose repress

285 se, the enzyme involved in the final step of heme synthesis, is deficient in these patients.

286 through ferritin, which resulted in reduced heme synthesis, reduced hemoglobin formation, and pertur

287 se (ALAS), which catalyzes the first step of heme synthesis.

288 red with the kinetics of CO binding in other heme systems such as myoglobin (Mb) and hemoglobin (Hb).

289 Of note, heme that was covalently bound to HemW was actively tran

290 , NIR FPs utilize an enzymatic derivative of heme, the linear tetrapyrrole biliverdin, as a chromopho

291 Although DGCR8 is known to bind heme, the molecular role of heme in pri-miR processing i

292 strated that MsrQ is able to bind two b-type hemes through the histidine residues conserved between t

293 Hemopexin protects against heme toxicity in hemolytic diseases and conditions, seps

294 red for HemW dimerization and HemW-catalyzed heme transfer but not for stable heme binding.

295 We propose a model for IsdB heme transfer from Hb that involves unfolding of Hb and

296 ional rearrangement and its implications for heme transfer via site-directed mutagenesis, resonance R

297 r iron homeostasis is maintained by iron and heme transport proteins that work in concert with ferrir

298 ics in heme binding and release in bacterial heme transport proteins.

299 types handle iron, highlighting how iron and heme transporters mediate the exchange and distribution

300 mitochondria in calcium handling, apoptosis, heme turnover, inflammation, and oxygen and nutrient sen