ライフサイエンスコーパス: prosthetic group

1 ve site above the distal surface of the heme prosthetic group.

2 cinimidyl-4-(18)F-fluorobenzoate ((18)F-SFB) prosthetic group.

3 ntains a single [4Fe-4S] cluster as its sole prosthetic group.

4 0-ACP) attached to the 4'-phosphopantetheine prosthetic group.

5 position that does not contact the bound FAD prosthetic group.

6 nzyme from Escherichia coli that removed the prosthetic group.

7 ar ACP and the slow turnover of the inactive prosthetic group.

8 mical environment of its linear tetrapyrrole prosthetic group.

9 onic hydroquinone form of the reduced flavin prosthetic group.

10 ctly to the isoalloxazine portion of the FAD prosthetic group.

11 ve rise to a mature PSD harboring a pyruvoyl prosthetic group.

12 aemprotein as the functionally indispensable prosthetic group.

13 sessing a tryptophan tryptophylquinone (TTQ) prosthetic group.

14 ne residue to reside within 30 A of the heme prosthetic group.

15 eractions of the protein with the large heme prosthetic group.

16 acquisition and endogenous synthesis of this prosthetic group.

17 bstrate-binding cavity formed above the heme prosthetic group.

18 es that use a covalently bound pyruvate as a prosthetic group.

19 kDa subunits that do not possess a corrinoid prosthetic group.

20 ossesses an organometallic nickel-containing prosthetic group.

21 depends critically on retention of the heme prosthetic group.

22 e proximal pocket beneath ring C of the heme prosthetic group.

23 t possesses the tryptophan tryptophylquinone prosthetic group.

24 affinity of the flavin-adenine dinucleotide prosthetic group.

25 d at blocking the production of the pyruvoyl prosthetic group.

26 single polypeptide chain and a single Fe2S2 prosthetic group.

27 f the protein that leads to solvation of the prosthetic group.

28 by binding of nitric oxide (*NO) to the heme prosthetic group.

29 r of a beta-hydride equivalent to the flavin prosthetic group.

30 containing a noncovalently bound b-type heme prosthetic group.

31 in charge-transfer interaction with the FMN prosthetic group.

32 tion of a beta-hydride equivalent to the FAD prosthetic group.

33 as a metabolic intermediate rather than as a prosthetic group.

34 6 is hydrogen-bonded to C(4)-O of the flavin prosthetic group.

35 binding motif for the ADP moiety of the FAD prosthetic group.

36 protein environment for the phytochromobilin prosthetic group.

37 rrelated with the oxidation state of the FMN prosthetic group.

38 attachment or the state of acylation of the prosthetic group.

39 e with a narrow constriction in front of the prosthetic group.

40 fur center rather than a pyridoxyl phosphate prosthetic group.

41 n flexibility and interactions with the heme prosthetic group.

42 variants analyzed led to a loss of the heme prosthetic group.

43 ost iron in mammals is found within the heme prosthetic group.

44 f lysozyme, a well-studied protein lacking a prosthetic group.

45 iates attached via the 4'-phosphopantetheine prosthetic group.

46 the C(15)=C(16) methine bridge of the bilin prosthetic group.

47 irectly by the 4-methylidene-imidazole-5-one prosthetic group.

48 cinimidyl-4-(18)F-fluorobenzoate ((18)F-SFB) prosthetic group.

49 ss Fe(2+) or Fe/S complexes as co-factors or prosthetic groups.

50 g, and that the folding can be stabilised by prosthetic groups.

51 generating patterns from proteins with rigid prosthetic groups.

52 tion of 3D patterns from proteins with rigid prosthetic groups.

53 n expression based on primary amine-reactive prosthetic groups.

54 Fe-2S] and flavin adenine dinucleotide (FAD) prosthetic groups.

55 t component of sMMO and the only one without prosthetic groups.

56 The enzyme contains three heme prosthetic groups.

57 ion using click tethering of fluorophores as prosthetic groups.

58 ts, have several disulfide bonds, or contain prosthetic groups.

59 to Compound II, which has Fe(IV) in its heme prosthetic groups.

60 cysteine-linked linear tetrapyrrole (bilin) prosthetic groups.

61 perty of all small globular proteins without prosthetic groups.

62 in the synthesis of Fe/S clusters and heme a prosthetic groups.

63 complexes associated with a small number of prosthetic groups.

64 atform is demonstrated by the thiol-specific prosthetic group, [(18)F]FPEGMA, which was used to produ

65 inct component activities and a site for the prosthetic group 4'-phosphopantetheine (acyl carrier pro

66 onal only when modified by attachment of the prosthetic group, 4'-phosphopantetheine (4'-PP), which i

67 was produced by a 2-step procedure with the prosthetic group 6-(18)F-fluoronicotinic acid 2,3,5,6-te

68 in this 2013 series deal with the molybdenum prosthetic group (a pterin known as Moco); the biosynthe

69 rostatic interactions of a compound with the prosthetic group allows the prediction of inhibitory pot

70 The prosthetic group alternates between methylcobalamin and

71 Each domain retains their prosthetic groups although the FMN domain is more labile

72 ls induced changes in resonances of the heme prosthetic group and an internal heme edge side chain, w

73 ess in which the heme participates both as a prosthetic group and as a substrate.

74 ence of Trp 22, and the other binds the heme prosthetic group and can be tracked via heme absorbance.

75 a very polar environment distal to its heme prosthetic group and contains a glutamic acid residue in

76 o help identify protein residues involved in prosthetic group and dimeric interaction, we expressed H

77 ompact structure enclosing the single haem c prosthetic group and leaving one edge of the haem expose

78 erone into progesterone acetate using FAD as prosthetic group and NADPH as reducing cofactor.

79 cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, readying them to ac

80 -Cys48 metal cluster binding loop around the prosthetic group and shifting of the metal center toward

81 ch contains the molecule coelenterazine as a prosthetic group and shows considerable potential in thi

82 to PDP1 or PDP1c requires the lipoyl-lysine prosthetic group and specificity residues that distingui

83 show that both DosS and DosT bind heme as a prosthetic group and that DosS is rapidly autooxidized t

84 hat both PAS domains of NPAS2 bind heme as a prosthetic group and that the heme status controls DNA b

85 the existence of covalent bonds between the prosthetic group and the protein, which has a strong imp

86 to form thioether linkages between the heme prosthetic group and the protein.

87 the oxidative capacity inherent in the heme prosthetic group and the specific binding behavior of ar

88 dependent haloperoxidases contain a vanadate prosthetic group and utilize hydrogen peroxide to oxidiz

89 HMP), which contains one heme and one FAD as prosthetic groups and is capable of reducing O(2) by its

90 features to be included, e.g. novel ligands, prosthetic groups and post-translational/transcriptional

91 he interaction between their respective heme prosthetic groups and protein environments, and in the a

92 fference spectra arise from perturbations of prosthetic groups and surrounding protein.

93 zymes in this process, one based on haem cd1 prosthetic groups and the other on type 1-type 2 Cu cent

94 DL-6,8-Thioctic acid (PDH prosthetic group) and insulin slightly augmented metabol

95 for the local atomic environment of the heme prosthetic group, and comparing the theoretically genera

96 is of the tryptophan tryptophylquinone (TTQ) prosthetic group, and formation of several structural di

97 monooxygenases, contains a tightly bound FAD prosthetic group, and is required for the stereoselectiv

98 ) redox couple of a covalently attached heme prosthetic group, and it has served as a paradigm for bo

99 n are indicative of protein-protein, protein-prosthetic group, and protein-lipid interactions.

100 1) range where vibrational bands of ligands, prosthetic groups, and protein and amino acid side chain

101 )F]fluorine, peptides are radiolabeled via a prosthetic group approach.

102 olded Cyt c and its covalently attached heme prosthetic group are translocated to the central chamber

103 G-protein-coupled receptor ligands and prosthetic groups are also being resolved using NMR meth

104 Prosthetic groups are often important structural organiz

105 Three prosthetic groups are present in the b6f complex that ar

106 ement outside the core and the complement of prosthetic groups are strikingly different.

107 containing eight subunits and seven natural prosthetic groups, are separated by a large lipid-contai

108 Aer may use its FAD prosthetic group as a cellular redox sensor to monitor e

109 large, modular enzyme that uses a cobalamin prosthetic group as a donor or acceptor in three separat

110 he isoalloxazine ring of an enzyme-bound FMN prosthetic group as a hydride, and an active site base (

111 lated to function on distal side of the heme prosthetic group as an acid-base catalyst in facilitatin

112 ulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occu

113 We identify heme, an iron-containing prosthetic group, as a regulatory ligand controlling hum

114 rrier protein (MdcC subunit) with a distinct prosthetic group, as well as decarboxylase (MdcD-MdcE) a

115 d a smaller alpha-subunit, which harbors the prosthetic group at its N terminus.

116 and together bind two flavin mononucleotide prosthetic groups at the dimer interface.

117 dopsin, i.e., bacterioopsin with the retinal prosthetic group attached, and to bacterioopsin associat

118 contains two flavin residues as redox-active prosthetic groups attached by a phosphoester bond to thr

119 olynucleotide phosphorylase and PTAC12), and prosthetic group attachment (HCF208/CCB2).

120 P from fabF strains occurred irrespective of prosthetic group attachment or the state of acylation of

121 emperature cannot be attributed to a lack of prosthetic group attachment.

122 Heme is a prosthetic group best known for roles in oxygen transpor

123 omplex homo-tetrameric enzymes with one heme prosthetic group buried in each subunit.

124 d heme oxygenase enzymes share a common heme prosthetic group but catalyze fundamentally different re

125 formation requires incorporation of the heme prosthetic group but does not require myristoylation or

126 as binding motifs for heme, FAD, and NAD(P)H prosthetic groups but no membrane anchor.

127 The simplest contain protohaem as sole prosthetic group, but show considerable variation in the

128 understood, and most heme proteins bind the prosthetic group by iron ion ligation and tertiary inter

129 Formation of the cob(II)alamin prosthetic group by oxidation of cob(I)alamin or photoly

130 Molybdoenzymes are ubiquitous and require a prosthetic group called the molybdenum cofactor for acti

131 anchor of E. coli QFR lacks heme; thus, this prosthetic group can be excluded as a spin relaxation en

132 m for the rapid preparation of water-soluble prosthetic groups capable of efficiently introducing (18

133 ly on using traditional metal ion chelate or prosthetic group chemistries.

134 Iron-sulfur clusters are prosthetic groups composed of sulfur and iron that are f

135 group is transferred from the substrate to a prosthetic group comprised of an amino acid triad in the

136 Iron-sulfur (Fe-S) proteins contain prosthetic groups consisting of two or more iron atoms b

137 molybdenum, iron, and acid-labile sulfur as prosthetic group constituents.

138 MetH(2-649) protein, which lacks a cobalamin prosthetic group, contain 0.9 equiv of zinc, while the C

139 tated the distance between the catalytic MIO prosthetic group created from (189)Ala-Ser-Gly(191) resi

140 In mitochondria FeS clusters, prosthetic groups critical for the activity of many prot

141 purified PGHS, including binding to its heme prosthetic group, cysteines, and tyrosyl radicals.

142 nally high binding affinity for an essential prosthetic group, D-biotin.

143 The prosthetic groups did have an effect; metabolites with s

144 soluble, functional molecules, complete with prosthetic groups, disulfide bonds, and quaternary struc

145 The heme prosthetic group does not appear to become modified, sin

146 cture of the wild-type FMO revealed that the prosthetic group FAD is an integral part of the protein.

147 electron-transfer proteins that contain the prosthetic group flavin mononucleotide.

148 n bonds to the O2 and N3 of the flavoprotein prosthetic group, FMN.

149 s synthesis featured fluorination of a novel prosthetic group, followed by a copper-free click conjug

150 Pyrroloquinoline quinone (PQQ), a prosthetic group for apoglucose dehydrogenase (apo-GDH),

151 Siroheme, the prosthetic group for both nitrite and sulfite reductases

152 ofolate dehydrogenase (FDH), requires a 4-PP prosthetic group for catalysis.

153 an iron-containing porphyrin that serves as prosthetic group for enzymes involved in oxidative metab

154 needs NADPH as a cofactor in addition to the prosthetic group for its catalytic activity.

155 Fe-S clusters are critical prosthetic groups for proteins involved in various criti

156 Haems are metalloporphyrins that serve as prosthetic groups for various biological processes inclu

157 We find that only 2 of 28 crosslink-free, prosthetic-group-free, chemically denatured polypeptides

158 phoresis conditions that readily release the prosthetic group from other non-CYP4 P450 isoforms.

159 The heme prosthetic group from the bovine milk enzyme lactoperoxi

160 in mammalian peroxidases is to protect their prosthetic group from their highly reactive metabolic pr

161 e thiolation domains with phosphopantetheine prosthetic groups, GliP activates and tethers l-Phe on T

162 , and triethylene glycol) and found that the prosthetic group has a significant effect on the in vitr

163 flavin mononucleotide (FMN) molecule as its prosthetic group, has a redox potential for the oxidized

164 hich was prepared using a [(18)F]fluoroethyl prosthetic group, has significant uptake in the myocardi

165 Silicon-containing prosthetic groups have been conjugated to peptides to al

166 The oxygenated and reduced forms of the prosthetic group help stabilize interactions with cofact

167 al for the incorporation of the redox-active prosthetic groups (heme b, heme b(3 )and Cu) into the cy

168 majority of iron is enclosed within a single prosthetic group: heme.

169 Redox responses associated with the heme prosthetic group in a myoglobin-polymer surfactant solve

170 onor and contain an Fe-S cluster as the sole prosthetic group in addition to the active-site disulfid

171 ing, tetrapyrrole ring, heme is an essential prosthetic group in an array of proteins that comprehens

172 To dissect the role of the heme prosthetic group in forcing the disordered region into t

173 Apart from serving as a prosthetic group in globins and enzymes, heme is a key r

174 c properties and electronic structure of the prosthetic group in high-spin, ferrous deoxy myoglobin f

175 if is critical for incorporation of the heme prosthetic group in human and rabbit CYP4B1 proteins exp

176 Heme is a required prosthetic group in many electron transfer proteins and

177 Following radioiodination of the TPP-based prosthetic group in phosphate buffer, the prosthetic gro

178 Heme is an essential prosthetic group in proteins that reside in virtually ev

179 orphyrin ring and functioning primarily as a prosthetic group in proteins.

180 Analysis of the prosthetic group in the CYP4F5 G330E mutant, into which

181 one of the functions of heme c(n), the only prosthetic group in the electron transport chain with ox

182 s function despite the absence of the heme B prosthetic group in the membrane.

183 Resonance Raman data show that the heme prosthetic group in the NO-bound hIDO is situated in a u

184 ere used to establish the orientation of the prosthetic group in the polypeptide matrix.

185 The data indicate that the diiron prosthetic group in vaccinia RR is assembled from iron t

186 hough it is required for turnover of the ACP prosthetic group in vivo.

187 of ordered water molecules that may act like prosthetic groups in a manner quite unlike bulk water.

188 its that contained no metal centers or other prosthetic groups in its as-isolated form.

189 The orientation of prosthetic groups in membrane proteins is of considerabl

190 Fe4S4 clusters are very common versatile prosthetic groups in proteins.

191 ses, indeed, show that one of the three heme prosthetic groups in the enzyme, heme b(595), is specifi

192 o results in covalent alteration of the heme prosthetic group, in part, to products that contain an i

193 2 results in covalent alteration of the heme prosthetic group, in part, to protein-bound adducts.

194 Structural water molecules may act as prosthetic groups indispensable for proper protein funct

195 rization reaction also influences the flavin prosthetic group inducing deprotonation to the green ani

196 e source, affirming that acetylation of this prosthetic group is an essential mechanistic step for ac

197 lasm of gram-negative bacteria, and the heme prosthetic group is covalently bound to the protein.

198 e b-type heme protein in which the porphyrin prosthetic group is covalently ligated to the polypeptid

199 denosine diphosphate (ADP) moiety of the FAD prosthetic group is displaced into the corresponding ADP

200 fer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for these tu

201 By contrast, the phosphopantetheine prosthetic group is not required for membrane-derived ol

202 xidation and hemin loss, indicating that the prosthetic group is readily accessible to solvent.

203 The prosthetic group is reduced upon anaerobic addition of H

204 , but labeling with conventional (18)F-based prosthetic groups is problematic due to long synthesis t

205 Insertion of prosthetic groups is usually spontaneous, and implies an

206 s contributed by the universal lipoyl-lysine prosthetic group, key specificity residues, and some con

207 h a region of the molecule that contains the prosthetic group lipoic acid (LA).

208 tion and analytical characteristics of novel prosthetic group loaded polymeric nanospheres for use in

209 n documented that catalytic and redox-active prosthetic groups may be derived from post-translational

210 The idea of water as a prosthetic group mediating chemical reaction dynamics is

211 s 650-896 are responsible for binding of the prosthetic group methylcobalamin, and amino acids 897-12

212 The enzyme contained the prosthetic group, molybdopterin guanine dinucleotide, an

213 te the overall reaction, the tethered biotin prosthetic group must first gain access to the biotin ca

214 The prosthetic group N-[2-(4-(18)F-fluorobenzamido) ethyl] m

215 e (FB)-anti-MMR sdAb was developed using the prosthetic group N-succinimidyl-4-(18)F-fluorobenzoate (

216 The 4'-phosphopantetheine prosthetic group of a holo-ACP is a long and flexible ar

217 Chelation of the copper ion of the prosthetic group of A4V prevented GLT1 inhibition.

218 Heme A is a prosthetic group of all eukaryotic and some prokaryotic

219 tween the tryptophan tryptophylquinone (TTQ) prosthetic group of aromatic amine dehydrogenase (AADH)

220 The heme prosthetic group of cytochrome c is covalently attached

221 Heme A, a prosthetic group of cytochrome c oxidase [EC 1.9.3.1], h

222 ntial for the biosynthesis of heme d(1), the prosthetic group of dissimilatory nitrite reductases in

223 that flavine adenine dinucleotide (FAD), the prosthetic group of GR, may be responsible for the enzym

224 The heme prosthetic group of heme proteins contains iron, which c

225 nd oxidative metabolism, most notably as the prosthetic group of hemoglobin and cytochromes.

226 required as one source of iron for the heme prosthetic group of KatA and thus for protection against

227 The covalently bound prosthetic group of lactoperoxidase (LPO) has been obtai

228 is of the tryptophan tryptophylquinone (TTQ) prosthetic group of MADH.

229 The heme molecule is the prosthetic group of many hemeproteins involved in essent

230 Tryptophan tryptophylquinone (TTQ), the prosthetic group of methylamine dehydrogenase, is formed

231 nthesis of tryptophan tryptophylquinone, the prosthetic group of methylamine dehydrogenase.

232 ne and specifically methylates the corrinoid prosthetic group of MtbC, which is subsequently demethyl

233 e biosynthesis of the "M-cluster" molybdenum prosthetic group of nitrogenase; the biosynthesis of the

234 ase of autoinhibitory NO. coordinated to the prosthetic group of nNOS, which, in conjunction with an

235 er of the inhibitor fluorescence to the heme prosthetic group of PGHS, we determined these inhibitors

236 DNA-tagged liposomes encapsulating PQQ, the prosthetic group of the apo-enzyme glucose dehydrogenase

237 sulating pyrroloquinoline quinone (PQQ), the prosthetic group of the apoenzyme glucose dehydrogenase

238 se required for the synthesis of heme a, the prosthetic group of the catalytic center of COX.

239 The FAD prosthetic group of the ERV/ALR family of sulfhydryl oxi

240 synthesis of the linear tetrapyrrole (bilin) prosthetic groups of cyanobacterial phytochromes and the

241 ith the binding of dioxygen (O2) to the heme prosthetic groups of the globin chains: from paramagneti

242 The bilin prosthetic groups of the phytochrome photoreceptors and

243 rapyrrole precursors of the light-harvesting prosthetic groups of the phytochrome photoreceptors of p

244 er protein and D-alanyl carrier protein, the prosthetic groups of which are derived from CoA.

245 However, the lipoyl prosthetic group on E2b is not essential for BDP binding

246 n open cleft leading to the active-site heme prosthetic group on the distal surface that is likely to

247 It is known that NO binds to a haem prosthetic group on the receptor and triggers a conforma

248 imeric form of MCR contains two Ni(I)-F(430) prosthetic groups, one in each monomer.

249 de (C62-C65) poised to interact with the FAD prosthetic group, only flavin reduction is evident durin

250 y physiological processes acting either as a prosthetic group or as an intracellular messenger.

251 n protein lacking prolines, disulfide bonds, prosthetic groups, or other gross structural features th

252 rm of the enzyme, on the other hand, lacks a prosthetic group other than its molybdenum center and ut

253 he first four pathways require the protein's prosthetic group, phosphopantetheine, to assemble an acy

254 valent attachment of the linear tetrapyrrole prosthetic group phytochromobilin.

255 These observations suggest that the prosthetic group plays a significant role in determining

256 F-labeled rhodamine B using three additional prosthetic groups (propyl, diethylene glycol, and trieth

257 provide evidence that addition of the biotin prosthetic group reduces the ability of BCCP Delta 67 to

258 The 4alpha-hydroperoxyflavin form of the prosthetic group represents a transient intermediate of

259 region responsible for binding the cobalamin prosthetic group (residues 650-896), and an AdoMet-bindi

260 energy transfer (FRET) studies in which heme prosthetic groups serve as acceptors.

261 Rhodopsin is unusual in that its retinal prosthetic group serves as an antagonist in the dark in

262 general for autocatalytic additions to heme prosthetic groups, suggests that meso hydroxylation of t

263 sulfite oxidase possess a b-type cytochrome prosthetic group that accepts reducing equivalents from

264 change in response to CO binding to its heme prosthetic group that allows it to bind specific DNA seq

265 possesses a cysteine tryptophylquinone (CTQ) prosthetic group that catalyzes the oxidative deaminatio

266 For this approach, a purpose-designed prosthetic group that incorporated both a radioiodinatab

267 Sirohaem is a tetrapyrrole-derived prosthetic group that is required for the essential assi

268 These enzymes contain heme prosthetic groups that are ligated through a histidine n

269 Iron-sulfur clusters are prosthetic groups that are required for the function of

270 ters are ubiquitous and evolutionary ancient prosthetic groups that are required to sustain fundament

271 Hemes are prosthetic groups that participate in diverse biochemica

272 n the CYP4 family covalently bind their heme prosthetic group to a conserved acidic I-helix residue v

273 oorotate (DHO) to orotate (OA) using the FMN prosthetic group to abstract a hydride equivalent from C

274 ihydroorotate (DHO) to orotate using the FMN prosthetic group to abstract a hydride equivalent from C

275 :FNRox) complexes or with the ability of the prosthetic group to be reduced by dRfH..

276 e rapidly after red cell lysis, allowing the prosthetic group to be removed by serum albumin and apoh

277 reductase family and can use FMN or FAD as a prosthetic group to catalyze reductive decyanation.

278 distance, allowing repositioning of the FMN prosthetic group to form new interactions that replace t

279 ight use a flavin adenine dinucleotide (FAD) prosthetic group to monitor cellular redox changes.

280 Most commonly it binds as a prosthetic group to proteins, and it has been widely sup

281 ctionalized with different iodine-containing prosthetic groups to generate a library of candidate cat

282 -tagged liposomes containing an encapsulated prosthetic group tracer, pyrroloquinoline quinone (PQQ),

283 llum rubrum, in which CO binding to its heme prosthetic group triggers a conformational change of Coo

284 nguish between proteins containing different prosthetic groups (unless they have different sequences)

285 ed prosthetic group in phosphate buffer, the prosthetic group was purified and coupled to the termina

286 fluoro-2-pentafluorophenyl naphthoate (PFPN) prosthetic group was synthesized to incorporate fluorine

287 e redox properties of its b- and c-type heme prosthetic groups were unchanged.

288 trates and analogues interact with heme, the prosthetic group which activates oxygen for the catalyti

289 ed that these proteins possess a b-type heme prosthetic group which is noncovalently bound at the act

290 a and beta subunits and forming the pyruvate prosthetic group, which is derived from an internal Ser

291 composed of an apoprotein moiety and a heme prosthetic group, which is required for CYP450 activity.

292 nine dinucleotide cofactor (MGD) as its sole prosthetic group, which is required for the reduction of

293 cture includes 16 subunits and more than 200 prosthetic groups, which are mostly light harvesting pig

294 rom NADH to ubiquinone through protein-bound prosthetic groups, which is coupled to the translocation

295 loped to replace a native noncovalent flavin prosthetic group with a covalently attached flavin analo

296 Typical cytochrome P450s secure the heme prosthetic group with a cysteine thiolate ligand bound t

297 sition 18 after oxidation of the ferric heme prosthetic group with peroxide.

298 e, particularly the interference of the heme prosthetic group with the tissue oxidant/antioxidant bal

299 Extensive interactions of the lipoyl-lysine prosthetic group within the active site are supported by

300 unusual decarboxylase containing a pyruvoyl prosthetic group within the active site.

301 of substantial perturbations (i.e., the heme prosthetic group) without the formation of deep misfolde