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1 genera such as Escherichia, Shewanella, and Rhodobacter, although TMAO reductases are present in man
2 se (CcO) and homologous prokaryotic forms of Rhodobacter and Paraccocus differ in the EPR spectrum of
4 ion of the formate dehydrogenase enzyme from Rhodobacter capsulatus (RcFDH) by means of hydrophobic i
6 oordinating the positioning of succinyl-CoA, Rhodobacter capsulatus ALAS Asn-85 has a proposed role i
8 n reported to encode C-8 vinyl reductases in Rhodobacter capsulatus and Arabidopsis thaliana, respect
9 tic basis of GTA production in the bacterium Rhodobacter capsulatus and characterization of novel pha
11 wn to complement RubisCO deletion strains of Rhodobacter capsulatus and Rhodobacter sphaeroides under
12 n is greatly repressed in a B12 auxotroph of Rhodobacter capsulatus and that B12 regulation of gene e
13 d and reduced wild-type cytochrome c(2) from Rhodobacter capsulatus and the lysine 93 to proline muta
14 ics of wild-type xanthine dehydrogenase from Rhodobacter capsulatus and variants at Arg-310 in the ac
16 rg/Glu135Arg mutants of Escherichia coli and Rhodobacter capsulatus bacterioferritins are unable to a
18 by the heme ligation core complex, which in Rhodobacter capsulatus contains at least the CcmF, CcmH,
19 rein we studied Zn(2+)-induced inhibition of Rhodobacter capsulatus cyt bc(1) using enzyme kinetics,
21 dues in the cytochrome c(1) component of the Rhodobacter capsulatus cytochrome bc(1) complex, phenyla
22 on chemistry and spectroscopic properties of Rhodobacter capsulatus cytochrome c' (RCCP) have been co
23 ations at 9 positions in the hinge region of Rhodobacter capsulatus cytochrome c(2) and have determin
25 he dissociation constants for the binding of Rhodobacter capsulatus cytochrome c2 and its K93P mutant
26 RC) mutants created in the background of the Rhodobacter capsulatus D(LL) mutant, in which the D heli
27 R. sphaeroides dimethyl sulfoxide reductase, Rhodobacter capsulatus dimethyl sulfoxide reductase, and
28 nanosecond flash photolysis and RCs from the Rhodobacter capsulatus F(L181)Y/Y(M208)F/L(M212)H mutant
30 dentified the small terminase from the model Rhodobacter capsulatus GTA, which then allowed predictio
31 molybdenum-containing Me(2)SO reductase from Rhodobacter capsulatus have been examined spectroscopica
32 Q variant of the xanthine dehydrogenase from Rhodobacter capsulatus have been examined to ascertain w
33 or selection in a Rubisco deletion strain of Rhodobacter capsulatus identified a residue in the amino
37 onstrate that the expression of hem genes in Rhodobacter capsulatus is transcriptionally repressed in
39 n center has been trapped in two D(LL)-based Rhodobacter capsulatus mutants that have Tyr at position
43 e P(+)Q(B)(-) is created in this manner in a Rhodobacter capsulatus RC containing the F(L181)Y-Y(M208
45 , V, F, H, K, and Q in purple photosynthetic Rhodobacter capsulatus results in hydroquinone oxidation
49 e previously reported that mutant strains of Rhodobacter capsulatus that have alanine insertions (+nA
51 r-diameter gene transfer agents of bacterium Rhodobacter capsulatus that transfer random 4.5-kbp (1.5
52 to form cytochrome c, leading in the case of Rhodobacter capsulatus to the loss of photosynthetic pro
54 eps at the Qi-site of the cyt bc1 complex of Rhodobacter capsulatus using atomistic molecular dynamic
55 bacterial xanthine dehydrogenase (XDH) from Rhodobacter capsulatus was immobilized on an edge-plane
56 ubisco) employing the phototrophic bacterium Rhodobacter capsulatus was used to select a catalyticall
59 purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and is essential in controlling
61 In many Gram-negative bacteria, including Rhodobacter capsulatus, cytochrome c maturation (Ccm) is
63 with the phytoene desaturase gene (crtI) of Rhodobacter capsulatus, producing carotenoids with short
64 he closest known homolog is the bluB gene of Rhodobacter capsulatus, which is implicated in the biosy
73 e iron oxidoreductase of the photoferrotroph Rhodobacter ferrooxidans SW2 was cloned, purified, and c
74 nalysis, demonstrated that these strains and Rhodobacter massiliensis represent a new genus, "Haemato
75 y alpha- and beta- proteobacteria, including Rhodobacter, Methylibium, Rhodopseudomonas, Methyloversa
76 ls of Fe-removed/Zn-replaced RC protein from Rhodobacter ( R.) sphaeroides R26 were irradiated with v
80 eme a (H102) is hydrogen bonded to serine in Rhodobacter (S44) and Paraccocus CcOs, in contrast to gl
81 a three-gene operon (the foxEYZ operon) from Rhodobacter sp. strain SW2 that confers enhanced light-d
82 a8c that overall was most similar to that of Rhodobacter species but was quite distinct from that of
84 ynthase (HOS) and heme A synthase (HAS) from Rhodobacter sphaeroides (Cox10 and Cox15, respectively)
86 PS(EC)), Salmonella minnesota (LPS(SM)), and Rhodobacter sphaeroides (LPS(RS)) and examined their act
87 saccharide from the photosynthetic bacterium Rhodobacter sphaeroides (LPS-RS), a TLR4 inhibitor, prev
89 xes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc(1)), stabilized with the q
92 s impediment does not extend to Rubisco from Rhodobacter sphaeroides (RsRubisco)-a red-type Rubisco a
93 ); Mycobacterium tuberculosis (type II); and Rhodobacter sphaeroides (type III)] were tested for the
94 2 complexes from the photosynthetic bacteria Rhodobacter sphaeroides 2.4.1 and Rhodopseudomonas acido
95 catalyze 9M5-FuFA and 9D5-FuFA synthesis in Rhodobacter sphaeroides 2.4.1 and Rhodopseudomonas palus
96 ulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1 have been well studied ove
101 hemA gene codes for one of two synthases in Rhodobacter sphaeroides 2.4.1 which catalyze the formati
104 vitro binding of PrrA, a global regulator in Rhodobacter sphaeroides 2.4.1, to the PrrA site 2, withi
105 he facultative phototrophic proteobacterium, Rhodobacter sphaeroides 2.4.1, was custom-designed and m
110 The metabolically versatile purple bacterium Rhodobacter sphaeroides 2.4.3 is a denitrifier whose gen
113 ce of F6P) to the recombinant wild-type (WT) Rhodobacter sphaeroides adenosine 5'-diphosphate-(ADP)-g
114 previously observed in another TRAP-PBP (the Rhodobacter sphaeroides alpha-keto acid-binding protein)
116 4, and 2.5 angstrom resolution) of TSPO from Rhodobacter sphaeroides and a mutant that mimics the hum
117 uced secondary quinone acceptor (Q(B)(-)) in Rhodobacter sphaeroides and Blastochloris viridis RCs.
118 lity assemblies are available: the bacterium Rhodobacter sphaeroides and chromosome 16 of the mouse g
119 ltiple heme groups (diheme cytochrome c from Rhodobacter sphaeroides and Desulfovibrio vulgaris Hilde
121 xidases and by the respiratory oxidases from Rhodobacter sphaeroides and Paracoccus denitrificans).
122 l transcription regulator in purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and
125 the B12-binding domain family present in the Rhodobacter sphaeroides AppA protein binds heme and sens
127 n the photosynthetic reaction center (RC) of Rhodobacter sphaeroides are investigated by site-directe
128 window using the photosensory module of the Rhodobacter sphaeroides bacteriophytochrome BphG1 and th
131 on between the two identical active sites in Rhodobacter sphaeroides BchNB that drives sequential and
134 he mapping of the photosynthetic membrane of Rhodobacter sphaeroides by atomic force microscopy (AFM)
137 Anomalous difference Fourier analyses of Rhodobacter sphaeroides CcO crystals, with cadmium added
142 analysis of G78S, A200T and Delta F94-F98 in Rhodobacter sphaeroides confirmed and extended these obs
143 structure of a complex of BcsA and BcsB from Rhodobacter sphaeroides containing a translocating polys
144 measured in reaction centers from mutants of Rhodobacter sphaeroides containing a tyrosine residue ne
145 e of chromatophores isolated from strains of Rhodobacter sphaeroides containing light harvesting comp
146 erized light-harvesting complex 2 (LH2) from Rhodobacter sphaeroides containing the N = 7 carotenoid
147 on transfer were also studied in a series of Rhodobacter sphaeroides cyt bc(1) mutants involving resi
148 series of 21 mutants in the cyt b ef loop of Rhodobacter sphaeroides cyt bc1 were prepared to examine
150 ng methionine (M185) in cytochrome c1 of the Rhodobacter sphaeroides cytochrome bc1 complex with Lys
153 d characterization of a series of mutants in Rhodobacter sphaeroides designed to reduce Q(B) via the
154 center (RC) of the photosynthetic bacterium Rhodobacter sphaeroides determines the rate and free ene
155 e (ICM) development process was performed in Rhodobacter sphaeroides during adaptation from high-inte
156 ivo and in vitro evidence that the genome of Rhodobacter sphaeroides encodes functional enzymes for C
159 In the oxidized state both mutants of the Rhodobacter sphaeroides enzyme, D132A and K362M, show ov
162 the photosynthetic reaction center (RC) from Rhodobacter sphaeroides exhibits a cation-pi complex for
163 bilized at the Qi-site of the bc1 complex of Rhodobacter sphaeroides forms a hydrogen bond with a nit
168 osynthetic membrane of the purple phototroph Rhodobacter sphaeroides has been characterised to a leve
169 cture of the light-harvesting I complex from Rhodobacter sphaeroides has been examined by site-direct
170 R from the anoxygenic phototrophic bacterium Rhodobacter sphaeroides has been known as an oxygen- and
171 ic reaction center from the purple bacterium Rhodobacter sphaeroides has been modified such that the
172 ve protochlorophyllide reductase (DPOR) from Rhodobacter sphaeroides has been purified from an Azotob
173 the transcriptional antirepressor AppA from Rhodobacter sphaeroides has been studied in the light an
174 n of the photosynthetic reaction center from Rhodobacter sphaeroides has been studied through the cha
176 -electron tomography to the purple bacterium Rhodobacter sphaeroides has demonstrated a heretofore un
177 ochrome c oxidoreductase (EC 1.10.2.2)) from Rhodobacter sphaeroides have been characterized using el
181 containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides have yielded new insight into it
182 ons of this extra fragment were generated in Rhodobacter sphaeroides in an effort to investigate its
183 cyt bc (1) from the photosynthetic bacterium Rhodobacter sphaeroides in complex with the fungicide az
184 n of the cytochrome c2-docked bc1 complex in Rhodobacter sphaeroides in terms of an ensemble of favor
185 cture for a translocator protein (TSPO) from Rhodobacter sphaeroides in which some of the electron de
190 ranscriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV si
191 genes involved in photosystem development in Rhodobacter sphaeroides is dependent upon three major re
192 Z) of the facultative phototrophic bacterium Rhodobacter sphaeroides is induced upon a drop of oxygen
193 experiments have shown that ICM assembly in Rhodobacter sphaeroides is initiated at indentations of
194 for whole cells of photosynthetic bacterium Rhodobacter sphaeroides lacking cytochrome c(2) as natur
196 1O2, we show that the phototrophic bacterium Rhodobacter sphaeroides mounts a transcriptional respons
197 n proton translocation of the bc(1) complex, Rhodobacter sphaeroides mutants expressing His-tagged cy
198 gment in bacterial cytochrome bc(1) complex, Rhodobacter sphaeroides mutants expressing His-tagged cy
199 ragment in bacterial cytochrome bc1 complex, Rhodobacter sphaeroides mutants expressing His-tagged cy
200 ion of quinol in the cytochrome bc1 complex, Rhodobacter sphaeroides mutants, H198N and H111N, lackin
201 structure of the axial mutant (Met182Thr) of Rhodobacter sphaeroides nitrite reductase in which the a
202 idic residue near the protein surface (D132, Rhodobacter sphaeroides numbering) and leads to another
204 ater and a pair of arginines, R481 and R482 (Rhodobacter sphaeroides numbering), that interact direct
207 eled ubiquinones in the Q(A) binding site in Rhodobacter sphaeroides photosynthetic reaction centers.
208 vesting 1 (LH1) integral membrane complex of Rhodobacter sphaeroides provides a convenient model syst
209 f SgTAM to the l-tyrosine ammonia lyase from Rhodobacter sphaeroides provides insight into the struct
210 RC) from the photosynthetic purple bacterium Rhodobacter sphaeroides R-26 were determined by fitting
213 visible and near-infrared spectral region to Rhodobacter sphaeroides RCs to accurately track the timi
214 otein complexes, and used it to reconstitute Rhodobacter sphaeroides reaction center complexes, demon
215 s during photosynthesis have been studied in Rhodobacter sphaeroides reaction centers from wild type
216 namics relationship was also demonstrated in Rhodobacter sphaeroides reaction centers having inhibite
218 ctron conduction across the highly tractable Rhodobacter sphaeroides reaction centre is characterized
219 nding processes in cytochrome c oxidase from Rhodobacter sphaeroides reduced to different degrees wer
220 210 in the photosynthetic reaction center of Rhodobacter sphaeroides results in the generation of a f
221 action centers (RCs) of the purple bacterium Rhodobacter sphaeroides runs selectively over one of the
222 39T mutant of translocator protein TSPO from Rhodobacter sphaeroides should be used to 1.65 instead o
224 the photosynthetic reaction center (RC) from Rhodobacter sphaeroides shows contacts between hydrophob
227 The DNA sequences of chromosomes I and II of Rhodobacter sphaeroides strain 2.4.1 have been revised,
230 cale TRN model for the alpha-Proteobacterium Rhodobacter sphaeroides that comprises 120 gene clusters
233 by the photosynthetic alpha-proteobacterium Rhodobacter sphaeroides to procure the cobamide it needs
235 letion strains of Rhodobacter capsulatus and Rhodobacter sphaeroides under both photoheterotrophic an
237 The aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides utilizes two proton-input channe
238 n photosynthetic reaction centers (RCs) from Rhodobacter sphaeroides was achieved by polarization sel
239 c(2) (cyt) and the reaction center (RC) from Rhodobacter sphaeroides was studied by mutation (to Ala)
241 ter from the purple photosynthetic bacterium Rhodobacter sphaeroides were covalently conjugated to ea
242 subtilis (expressed in Escherichia coli) and Rhodobacter sphaeroides were examined by analysis of cel
243 n kinetics of reaction centers isolated from Rhodobacter sphaeroides were shown to be inherently biph
244 heme protein from a denitrifying variant of Rhodobacter sphaeroides which may serve to store and tra
245 d reaction centers from the purple bacterium Rhodobacter sphaeroides with different primary electron
246 ated Rieske fragment from the bc1 complex of Rhodobacter sphaeroides with nitrogens (14N and 15N) fro
247 crystals of cytochrome c oxidase (CcO) from Rhodobacter sphaeroides yield a previously unreported st
248 copper-containing nitrite reductase (NiR) of Rhodobacter sphaeroides yielded endogenous NO and the Cu
249 ome c(2) to photosynthetic reaction centers (Rhodobacter sphaeroides) has been measured to high preci
250 these chromatophores can be spherical (as in Rhodobacter sphaeroides), lamellar (as in Rhodopseudomon
253 several sources (bovine heart mitochondria, Rhodobacter sphaeroides, and Paracoccus denitrificans).
254 he absorption spectrum of intact vesicles in Rhodobacter sphaeroides, as well as the well-established
256 e facultatively phototrophic proteobacterium Rhodobacter sphaeroides, formation of the photosynthetic
257 ction center in chromatophore membranes from Rhodobacter sphaeroides, have allowed us to demonstrate
260 agged membrane protein, Reaction Center from Rhodobacter sphaeroides, performed 2400 crystallization
262 enter (RC) from the photosynthetic bacterium Rhodobacter sphaeroides, that function in intermolecular
263 In the photosynthetic reaction center from Rhodobacter sphaeroides, the primary (Q(A)) and secondar
264 otein, the light-harvesting LH2 complex from Rhodobacter sphaeroides, to patterned self-assembled mon
266 ying the carotenoidless mutant strain R26 of Rhodobacter sphaeroides, we demonstrate by experiment an
267 the photoheterotrophic alpha-proteobacterium Rhodobacter sphaeroides, we identified a surprising feat
268 low-light-adapted chromatophore vesicle from Rhodobacter sphaeroides, we investigate the cooperation
269 oxidized forms of cytochrome c oxidase from Rhodobacter sphaeroides, we observe a displacement of he
271 l1 and Mcl2, two malyl-CoA lyase homologs in Rhodobacter sphaeroides, were investigated by gene inact
272 d by the genome of the alpha-proteobacterium Rhodobacter sphaeroides, which synthesizes a mitochondri