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1 edox activity of individual purple bacteria (Rhodobacter sphaeroides).
2 rates photosynthetic growth in the bacterium Rhodobacter sphaeroides.
3 ion of AppA, an oxygen and light sensor from Rhodobacter sphaeroides.
4 olog, RpoH(II), in the alpha-proteobacterium Rhodobacter sphaeroides.
5 ase PrrB in response to low oxygen levels in Rhodobacter sphaeroides.
6 beta-apoprotein from the core LH complex of Rhodobacter sphaeroides.
7 photosynthesis in the alpha-proteobacterium Rhodobacter sphaeroides.
8 anoic acid) (19Fu-FA), in phospholipids from Rhodobacter sphaeroides.
9 bb operons, responsible for CO2 fixation, in Rhodobacter sphaeroides.
10 gulator of photosynthesis gene expression in Rhodobacter sphaeroides.
11 ic membranes from PufX+ and PufX- strains of Rhodobacter sphaeroides.
12 like that found in the alpha-proteobacterium Rhodobacter sphaeroides.
13 fixation pathway (cbbI and cbbII) operons of Rhodobacter sphaeroides.
14 ssion of adhI, the gene encoding GSH-FDH, in Rhodobacter sphaeroides.
15 esis gene expression in the purple bacterium Rhodobacter sphaeroides.
16 n a thriving culture of the purple bacteria, Rhodobacter sphaeroides.
17 genes of the Calvin-Benson-Bassham cycle of Rhodobacter sphaeroides.
18 (35% identity, 54% similarity) to PmtA from Rhodobacter sphaeroides.
19 s encoded in the second chemotaxis operon of Rhodobacter sphaeroides.
20 odified photosynthetic reaction centers from Rhodobacter sphaeroides.
21 iochlorophyll dimer in reaction centers from Rhodobacter sphaeroides.
22 oleucine at position 265 of the M subunit in Rhodobacter sphaeroides.
23 t regulate photosynthesis gene expression in Rhodobacter sphaeroides.
24 was studied in the reaction center (RC) from Rhodobacter sphaeroides.
25 ntrast and fluorescence microscopy images of Rhodobacter sphaeroides.
26 ed from purified BcsA and BcsB proteins from Rhodobacter sphaeroides.
27 been performed on cytochrome c oxidase from Rhodobacter sphaeroides.
28 oteins making up the split kinase, is met in Rhodobacter sphaeroides.
29 response of the bacterial reaction center of Rhodobacter sphaeroides.
30 film formation in the monotrichous bacterium Rhodobacter sphaeroides.
31 in detergent-solubilized bc(1) complex from Rhodobacter sphaeroides.
32 of mitochondria and many bacteria, including Rhodobacter sphaeroides.
33 h surprising similarity to the fla2 locus of Rhodobacter sphaeroides.
34 at high and low pH in nitrite reductase from Rhodobacter sphaeroides.
35 sfer in single reaction center crystals from Rhodobacter sphaeroides.
36 n-Bassham CO(2) fixation pathway) operons of Rhodobacter sphaeroides.
37 of similarity to the original pucBA genes of Rhodobacter sphaeroides 2.4.1 (designated puc1) was iden
38 2 complexes from the photosynthetic bacteria Rhodobacter sphaeroides 2.4.1 and Rhodopseudomonas acido
39 ulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1 have been well studied ove
44 he tryptophan-rich sensory protein (TspO) of Rhodobacter sphaeroides 2.4.1 were studied using site-di
45 hemA gene codes for one of two synthases in Rhodobacter sphaeroides 2.4.1 which catalyze the formati
49 vitro binding of PrrA, a global regulator in Rhodobacter sphaeroides 2.4.1, to the PrrA site 2, withi
50 he facultative phototrophic proteobacterium, Rhodobacter sphaeroides 2.4.1, was custom-designed and m
57 The metabolically versatile purple bacterium Rhodobacter sphaeroides 2.4.3 is a denitrifier whose gen
65 ce of F6P) to the recombinant wild-type (WT) Rhodobacter sphaeroides adenosine 5'-diphosphate-(ADP)-g
66 previously observed in another TRAP-PBP (the Rhodobacter sphaeroides alpha-keto acid-binding protein)
68 4, and 2.5 angstrom resolution) of TSPO from Rhodobacter sphaeroides and a mutant that mimics the hum
69 uced secondary quinone acceptor (Q(B)(-)) in Rhodobacter sphaeroides and Blastochloris viridis RCs.
70 lity assemblies are available: the bacterium Rhodobacter sphaeroides and chromosome 16 of the mouse g
72 xidases and by the respiratory oxidases from Rhodobacter sphaeroides and Paracoccus denitrificans).
73 nt amino acid sequence similarity to PrrA of Rhodobacter sphaeroides and related proteins in other al
74 l transcription regulator in purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and
77 several sources (bovine heart mitochondria, Rhodobacter sphaeroides, and Paracoccus denitrificans).
78 ribosomal RNAs from Rhodocyclus gelatinosa, Rhodobacter sphaeroides, and Pseudomonas cepacia were de
79 (Chromatium vinosum, Rhodospirillum rubrum, Rhodobacter sphaeroides, and Rhodocyclus gelatinosa), th
80 he cofactor and can efficiently reconstitute Rhodobacter sphaeroides apo-DMSOR, an enzyme that requir
81 the B12-binding domain family present in the Rhodobacter sphaeroides AppA protein binds heme and sens
84 g the putative H-channel in the oxidase from Rhodobacter sphaeroides are examined by site-directed mu
85 n the photosynthetic reaction center (RC) of Rhodobacter sphaeroides are investigated by site-directe
86 he absorption spectrum of intact vesicles in Rhodobacter sphaeroides, as well as the well-established
87 window using the photosensory module of the Rhodobacter sphaeroides bacteriophytochrome BphG1 and th
91 s study we show that the PpsR repressor from Rhodobacter sphaeroides binds to DNA in a redox-dependen
93 (VI) and reduced Mo(IV) forms of recombinant Rhodobacter sphaeroides biotin sulfoxide reductase expre
94 Conditions for heterologous expression of Rhodobacter sphaeroides biotin sulfoxide reductase in Es
95 he mapping of the photosynthetic membrane of Rhodobacter sphaeroides by atomic force microscopy (AFM)
99 logous expression experiments indicated that Rhodobacter sphaeroides CbbR responded to the same metab
100 Anomalous difference Fourier analyses of Rhodobacter sphaeroides CcO crystals, with cadmium added
101 chrome c oxidase (CcO) was studied using two Rhodobacter sphaeroides CcO mutants involving direct lig
109 analysis of G78S, A200T and Delta F94-F98 in Rhodobacter sphaeroides confirmed and extended these obs
111 structure of a complex of BcsA and BcsB from Rhodobacter sphaeroides containing a translocating polys
112 measured in reaction centers from mutants of Rhodobacter sphaeroides containing a tyrosine residue ne
113 e of chromatophores isolated from strains of Rhodobacter sphaeroides containing light harvesting comp
114 Reaction centers from the Y(L167) mutant of Rhodobacter sphaeroides, containing a highly oxidizing b
117 ynthase (HOS) and heme A synthase (HAS) from Rhodobacter sphaeroides (Cox10 and Cox15, respectively)
118 on transfer were also studied in a series of Rhodobacter sphaeroides cyt bc(1) mutants involving resi
119 series of 21 mutants in the cyt b ef loop of Rhodobacter sphaeroides cyt bc1 were prepared to examine
121 protein to cytochrome c(1) (cyt c(1)) in the Rhodobacter sphaeroides cytochrome bc(1) complex was stu
122 bc(1) complex was studied using a series of Rhodobacter sphaeroides cytochrome bc(1) mutants in whic
123 ng methionine (M185) in cytochrome c1 of the Rhodobacter sphaeroides cytochrome bc1 complex with Lys
124 Binding of zinc to the outside surface of Rhodobacter sphaeroides cytochrome c oxidase inhibits th
125 as engineered onto the C-terminal end of the Rhodobacter sphaeroides cytochrome c oxidase subunit II.
128 d characterization of a series of mutants in Rhodobacter sphaeroides designed to reduce Q(B) via the
129 center (RC) of the photosynthetic bacterium Rhodobacter sphaeroides determines the rate and free ene
130 guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase (DM
131 rate the Tyr-114 --> Ala and Phe variants of Rhodobacter sphaeroides DMSOR and insert a Tyr residue i
132 clarification of the active site of oxidized Rhodobacter sphaeroides DMSOR, we have adopted the minim
133 e (ICM) development process was performed in Rhodobacter sphaeroides during adaptation from high-inte
134 ivo and in vitro evidence that the genome of Rhodobacter sphaeroides encodes functional enzymes for C
137 In the oxidized state both mutants of the Rhodobacter sphaeroides enzyme, D132A and K362M, show ov
140 the photosynthetic reaction center (RC) from Rhodobacter sphaeroides exhibits a cation-pi complex for
144 s found in a subset of FNR homologs, such as Rhodobacter sphaeroides FnrL, resulted in a mutant strai
147 e facultatively phototrophic proteobacterium Rhodobacter sphaeroides, formation of the photosynthetic
148 bilized at the Qi-site of the bc1 complex of Rhodobacter sphaeroides forms a hydrogen bond with a nit
149 ight harvesting 1 antenna (LH1) complex from Rhodobacter sphaeroides funnels excitation energy to the
155 hyde oxidation in the facultative phototroph Rhodobacter sphaeroides has allowed the identification o
156 osynthetic membrane of the purple phototroph Rhodobacter sphaeroides has been characterised to a leve
157 cture of the light-harvesting I complex from Rhodobacter sphaeroides has been examined by site-direct
158 R from the anoxygenic phototrophic bacterium Rhodobacter sphaeroides has been known as an oxygen- and
159 ic reaction center from the purple bacterium Rhodobacter sphaeroides has been modified such that the
160 ve protochlorophyllide reductase (DPOR) from Rhodobacter sphaeroides has been purified from an Azotob
162 The structure of the reaction center from Rhodobacter sphaeroides has been solved by using x-ray d
163 the transcriptional antirepressor AppA from Rhodobacter sphaeroides has been studied in the light an
164 n of the photosynthetic reaction center from Rhodobacter sphaeroides has been studied through the cha
166 -electron tomography to the purple bacterium Rhodobacter sphaeroides has demonstrated a heretofore un
171 ome c(2) to photosynthetic reaction centers (Rhodobacter sphaeroides) has been measured to high preci
172 the pufX gene of Rhodobacter capsulatus and Rhodobacter sphaeroides, has been further characterized.
173 ochrome c oxidoreductase (EC 1.10.2.2)) from Rhodobacter sphaeroides have been characterized using el
177 containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides have yielded new insight into it
178 ction center in chromatophore membranes from Rhodobacter sphaeroides, have allowed us to demonstrate
179 ons of this extra fragment were generated in Rhodobacter sphaeroides in an effort to investigate its
180 n of the cytochrome c2-docked bc1 complex in Rhodobacter sphaeroides in terms of an ensemble of favor
181 cture for a translocator protein (TSPO) from Rhodobacter sphaeroides in which some of the electron de
184 center from the purple non-sulfur bacterium Rhodobacter sphaeroides is a quasi-symmetric heterodimer
187 ranscriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV si
188 itch between aerobic and anaerobic growth in Rhodobacter sphaeroides is controlled by the RegA/RegB t
189 genes involved in photosystem development in Rhodobacter sphaeroides is dependent upon three major re
190 Z) of the facultative phototrophic bacterium Rhodobacter sphaeroides is induced upon a drop of oxygen
191 experiments have shown that ICM assembly in Rhodobacter sphaeroides is initiated at indentations of
193 reductive pentose phosphate cycle operon of Rhodobacter sphaeroides is regulated by both the transcr
195 roles is 5-aminolevulinic acid (ALA), and in Rhodobacter sphaeroides its formation occurs via the She
196 these chromatophores can be spherical (as in Rhodobacter sphaeroides), lamellar (as in Rhodopseudomon
197 that the facultative phototrophic bacterium Rhodobacter sphaeroides, like the closely related Rhodob
200 saccharide from the photosynthetic bacterium Rhodobacter sphaeroides (LPS-RS), a TLR4 inhibitor, prev
201 mide gel electrophoresis at 4 degrees C from Rhodobacter sphaeroides M21, which lacks the peripheral
204 1O2, we show that the phototrophic bacterium Rhodobacter sphaeroides mounts a transcriptional respons
205 n proton translocation of the bc(1) complex, Rhodobacter sphaeroides mutants expressing His-tagged cy
206 gment in bacterial cytochrome bc(1) complex, Rhodobacter sphaeroides mutants expressing His-tagged cy
207 ragment in bacterial cytochrome bc1 complex, Rhodobacter sphaeroides mutants expressing His-tagged cy
208 ieske iron-sulfur proteins in solution, four Rhodobacter sphaeroides mutants expressing His-tagged cy
209 sulfur protein (ISP) during bc(1) catalysis, Rhodobacter sphaeroides mutants expressing His-tagged cy
210 ion of quinol in the cytochrome bc1 complex, Rhodobacter sphaeroides mutants, H198N and H111N, lackin
211 structure of the axial mutant (Met182Thr) of Rhodobacter sphaeroides nitrite reductase in which the a
213 idic residue near the protein surface (D132, Rhodobacter sphaeroides numbering) and leads to another
215 ater and a pair of arginines, R481 and R482 (Rhodobacter sphaeroides numbering), that interact direct
216 annel is well-defined as D132(I) (subunit I; Rhodobacter sphaeroides numbering), the entrance of the
218 bout 25 A from an aspartic acid (D132 in the Rhodobacter sphaeroides oxidase) near the cytoplasmic ("
220 agged membrane protein, Reaction Center from Rhodobacter sphaeroides, performed 2400 crystallization
221 eled ubiquinones in the Q(A) binding site in Rhodobacter sphaeroides photosynthetic reaction centers.
222 directed evolution to change the product of Rhodobacter sphaeroides phytoene desaturase (crtI gene p
223 The PrrBA two-component activation system of Rhodobacter sphaeroides plays a major role in the induct
225 vesting 1 (LH1) integral membrane complex of Rhodobacter sphaeroides provides a convenient model syst
226 f SgTAM to the l-tyrosine ammonia lyase from Rhodobacter sphaeroides provides insight into the struct
227 face site on native Fe2+-containing RCs from Rhodobacter sphaeroides R-26 and to the native non-heme
229 RC) from the photosynthetic purple bacterium Rhodobacter sphaeroides R-26 were determined by fitting
231 es of electron transfer between six modified Rhodobacter sphaeroides RCs in which negatively charged
232 visible and near-infrared spectral region to Rhodobacter sphaeroides RCs to accurately track the timi
233 ectrochemical midpoint potentials as Q(A) in Rhodobacter sphaeroides reaction centers (RCs) and in RC
234 s during photosynthesis have been studied in Rhodobacter sphaeroides reaction centers from wild type
235 f the primary electron-transfer processes in Rhodobacter sphaeroides reaction centers have been exami
237 ctron conduction across the highly tractable Rhodobacter sphaeroides reaction centre is characterized
238 nding processes in cytochrome c oxidase from Rhodobacter sphaeroides reduced to different degrees wer
239 in mitochondria and aerobic bacteria such as Rhodobacter sphaeroides requires the association of thre
240 hrome c(2) oxidoreductase (bc(1) complex) of Rhodobacter sphaeroides, residue Tyr 156 is located clos
241 210 in the photosynthetic reaction center of Rhodobacter sphaeroides results in the generation of a f
242 spectra of the aa3 cytochrome c oxidase from Rhodobacter sphaeroides reveal pH-dependent structural c
243 zed photosynthetic reaction center (RC) from Rhodobacter sphaeroides, revealed an RC concentration-de
244 ction centers (RCs) from the purple bacteria Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rho
247 xes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc(1)), stabilized with the q
249 ryl lipid A derived from the nontoxic LPS of Rhodobacter sphaeroides (RsDPLA) has been shown to be a
251 action centers (RCs) of the purple bacterium Rhodobacter sphaeroides runs selectively over one of the
252 39T mutant of translocator protein TSPO from Rhodobacter sphaeroides should be used to 1.65 instead o
254 the photosynthetic reaction center (RC) from Rhodobacter sphaeroides shows contacts between hydrophob
257 The DNA sequences of chromosomes I and II of Rhodobacter sphaeroides strain 2.4.1 have been revised,
261 cale TRN model for the alpha-Proteobacterium Rhodobacter sphaeroides that comprises 120 gene clusters
262 enter (RC) from the photosynthetic bacterium Rhodobacter sphaeroides, that function in intermolecular
265 In the photosynthetic reaction center from Rhodobacter sphaeroides, the primary (Q(A)) and secondar
267 In chromatophores of the purple bacterium Rhodobacter sphaeroides, this has been associated with t
269 by the photosynthetic alpha-proteobacterium Rhodobacter sphaeroides to procure the cobamide it needs
270 otein, the light-harvesting LH2 complex from Rhodobacter sphaeroides, to patterned self-assembled mon
271 ); Mycobacterium tuberculosis (type II); and Rhodobacter sphaeroides (type III)] were tested for the
274 letion strains of Rhodobacter capsulatus and Rhodobacter sphaeroides under both photoheterotrophic an
277 The aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides utilizes two proton-input channe
278 n photosynthetic reaction centers (RCs) from Rhodobacter sphaeroides was achieved by polarization sel
279 c(2) (cyt) and the reaction center (RC) from Rhodobacter sphaeroides was studied by mutation (to Ala)
281 ying the carotenoidless mutant strain R26 of Rhodobacter sphaeroides, we demonstrate by experiment an
282 low-light-adapted chromatophore vesicle from Rhodobacter sphaeroides, we investigate the cooperation
283 oxidized forms of cytochrome c oxidase from Rhodobacter sphaeroides, we observe a displacement of he
285 ter from the purple photosynthetic bacterium Rhodobacter sphaeroides were covalently conjugated to ea
286 subtilis (expressed in Escherichia coli) and Rhodobacter sphaeroides were examined by analysis of cel
287 ctivity to the three-subunit core complex of Rhodobacter sphaeroides were generated and characterized
288 (P) in the photosynthetic reaction center of Rhodobacter sphaeroides were investigated by introducing
289 n kinetics of reaction centers isolated from Rhodobacter sphaeroides were shown to be inherently biph
290 atase H subunits from both Synechocystis and Rhodobacter sphaeroides were studied because of the diff
291 center (RC) from the photosynthetic bacteria Rhodobacter sphaeroides were studied by using site-direc
293 l1 and Mcl2, two malyl-CoA lyase homologs in Rhodobacter sphaeroides, were investigated by gene inact
294 vered in the photosynthetic purple bacterium Rhodobacter sphaeroides where it seems to replace phosph
295 heme protein from a denitrifying variant of Rhodobacter sphaeroides which may serve to store and tra
296 d by the genome of the alpha-proteobacterium Rhodobacter sphaeroides, which synthesizes a mitochondri
297 reaction of cytochrome c oxidase (COX) from Rhodobacter sphaeroides with hydrogen peroxide has been
298 ated Rieske fragment from the bc1 complex of Rhodobacter sphaeroides with nitrogens (14N and 15N) fro
299 crystals of cytochrome c oxidase (CcO) from Rhodobacter sphaeroides yield a previously unreported st
300 copper-containing nitrite reductase (NiR) of Rhodobacter sphaeroides yielded endogenous NO and the Cu
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