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1 se domains of GlnD from Escherichia coli and Rhodospirillum rubrum.
2 r used in the anaerobic energy metabolism of Rhodospirillum rubrum.
3 imilar to those measured for native LH1 from Rhodospirillum rubrum.
4 ription of genes involved in CO oxidation in Rhodospirillum rubrum.
5 of the genes responsible for CO oxidation in Rhodospirillum rubrum.
6 oA is a dimeric CO-sensing heme protein from Rhodospirillum rubrum.
7 ructures, including the form II homolog from Rhodospirillum rubrum.
8 n identified in the photosynthetic bacterium Rhodospirillum rubrum.
9 rotein transcription factor of the bacterium Rhodospirillum rubrum.
10 hate for nonmevalonate isoprene synthesis in Rhodospirillum rubrum.
11 d previously in the photosynthetic bacterium Rhodospirillum rubrum.
12 mely, Rb. sphaeroides, P. denitrificans, and Rhodospirillum rubrum.
13 ired for utilizing CO as an energy source in Rhodospirillum rubrum.
14 of carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum.
15 nsformed by plasmids carrying dra genes from Rhodospirillum rubrum.
16 reductase ADP-ribosyltransferase (DRAT) from Rhodospirillum rubrum.
17 but resembles that of the CO sensor CooA of Rhodospirillum rubrum.
18 ethanosarcina barkeri, Escherichia coli, and Rhodospirillum rubrum.
19 of CO to CO(2) in the phototrophic bacterium Rhodospirillum rubrum.
20 complex (LH1) of Rhodobacter sphaeroides or Rhodospirillum rubrum.
21 the carbon monoxide dehydrogenase (CODH) of Rhodospirillum rubrum.
22 was with the membrane-bound hydrogenase from Rhodospirillum rubrum.
23 e consisting of alpha and beta subunits from Rhodospirillum rubrum and gamma subunit from spinach chl
25 regulatory system, has been characterized in Rhodospirillum rubrum and other nitrogen-fixing bacteria
26 the nonsulfur purple photosynthetic bacteria Rhodospirillum rubrum and Rhodobacter sphaeroides, conta
28 ylene formation in the phototrophic bacteria Rhodospirillum rubrum and Rhodopseudomonas palustris In
29 he photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum and the analysis of the roles of G
30 the highest identity with the cbbM gene from Rhodospirillum rubrum, and analysis of the inferred amin
31 quired cofactor for anaerobic respiration in Rhodospirillum rubrum, and it is also found in several h
33 the same mean diameter as the LH1 rings from Rhodospirillum rubrum ( approximately 90 A) and therefor
34 Nitrogen fixation is tightly regulated in Rhodospirillum rubrum at two different levels: transcrip
35 ammaC) and the cloned alpha subunit from the Rhodospirillum rubrum ATP synthase (alphaR) was assemble
36 n monoxide-sensing transcription factor from Rhodospirillum rubrum, binds CO at a reduced (Fe(II)) he
37 n monoxide-sensing transcription factor from Rhodospirillum rubrum, binds CO through a heme moiety re
38 Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum catalyzes both the oxidation of CO
39 , reduced, and CO-bound reduced forms of the Rhodospirillum rubrum CO oxidation transcriptional activ
41 Fe, whereas the same cluster in enzymes from Rhodospirillum rubrum (CODH(Rr)) and Moorella thermoacet
42 Carbon-monoxide dehydrogenase (CODH) from Rhodospirillum rubrum contains two metal centers: a Ni-X
43 ginine hydrolases from mammalian tissues and Rhodospirillum rubrum exhibit three regions of similarit
44 entoxin-insensitive photosynthetic bacterium Rhodospirillum rubrum F(1) (RrF(1)), was stimulated but
45 d together with alpha and beta subunits from Rhodospirillum rubrum F1 into a hybrid photosynthetic F1
46 (fMetTrpArg) of the LH1 alpha-polypeptide of Rhodospirillum rubrum form a cluster that is most likely
47 hesis of polyhydroxyalkanoates (PHAs) in the Rhodospirillum rubrum genome revealed by the occurrence
50 -S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum has been determined to 2.8-A resol
51 reductase ADP-ribosyltransferase (DRAT) from Rhodospirillum rubrum has been investigated with a cross
52 nifH mutant of the photosynthetic bacterium Rhodospirillum rubrum has been purified and characterize
53 (RC-LH1) of the purple non- sulfur bacterium Rhodospirillum rubrum have been formed from detergent-so
54 In carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum, histidine 265 was replaced with v
55 he CO-sensing transcriptional activator from Rhodospirillum rubrum, in which CO binding to its heme p
56 arbon monoxide, the photosynthetic bacterium Rhodospirillum rubrum induces expression of proteins whi
59 O enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an eno
60 BluB protein of the photosynthetic bacterium Rhodospirillum rubrum is necessary and sufficient for ca
61 tations that correct such growth problems in Rhodospirillum rubrum mutants lacking P(II) proteins.
64 ly partially understood, and we show that in Rhodospirillum rubrum one P(II) homolog, GlnJ, has highe
65 Here we show that denatured RuBisCO from Rhodospirillum rubrum populates a stable, nonaggregating
67 CO-responsive transcription factor CooA from Rhodospirillum rubrum provides evidence on the nature of
68 he CO-sensing transcriptional regulator from Rhodospirillum rubrum, reacts with NO to form a five-coo
72 in the purple bacteria (Chromatium vinosum, Rhodospirillum rubrum, Rhodobacter sphaeroides, and Rhod
73 of Rhodobacter sphaeroides (sph beta 31) or Rhodospirillum rubrum (rr beta 31) could form subunit-ty
74 eminate CO rebinding in two CooA homologues, Rhodospirillum rubrum (RrCooA) and Carboxydothermus hydr
76 t RuBP accumulation can impede the growth of Rhodospirillum rubrum (Rs. rubrum) and Rhodopseudomonas
77 of carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum show that CODH is mostly inactive
78 chia coli, thermophilic Bacillus strain PS3, Rhodospirillum rubrum, spinach chloroplasts, and the cya
79 rogenase reductases also were expressed in a Rhodospirillum rubrum strain that lacked its endogenous
82 NAD(H) binding alpha1 subunit (domain I) of Rhodospirillum rubrum TH have been determined at 1.8 A r
83 is a CO-sensing transcription activator from Rhodospirillum rubrum that binds specific DNA sequences
84 hat the H(+)-pyrophosphatase (H(+)-PPase) of Rhodospirillum rubrum, the first enzyme of this type tha
86 e-based sensor CooA regulates the ability of Rhodospirillum rubrum to grow on CO as an energy source.
87 ining transcriptional activator that enables Rhodospirillum rubrum to sense and grow on CO as a sole
89 dI and dIII (the dI(2)dIII(1) complex) from Rhodospirillum rubrum transhydrogenase catalyzes fast si
90 in the NAD(H)-binding component (dI) of the Rhodospirillum rubrum transhydrogenase was substituted w
91 designated H2NADH) bound to isolated dI from Rhodospirillum rubrum transhydrogenase with similar affi
93 ing homodimeric transcription activator from Rhodospirillum rubrum, undergoes a conformational change
94 Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum utilizes three types of Fe-S clust
96 hanism of the transcription factor CooA from Rhodospirillum rubrum was studied through a systematic m
97 protein from the CO dehydrogenase system of Rhodospirillum rubrum, was purified by immobilized metal
98 mutations and metabolomics in the bacterium Rhodospirillum rubrum, we show here that Rubisco concurr
99 ctase-activating glycohydrolase (DRAG), from Rhodospirillum rubrum, were shown to be sensitive to the
100 purified from the chromatophore membranes of Rhodospirillum rubrum with a 3,464-fold purification and
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