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1 genesis in Clostridium acetobutylicum and C. beijerinckii.
2 ation of CO2 and H2 by n-butanol-producer C. beijerinckii.
3 f mixotrophic inorganic carbon-capture by C. beijerinckii.
4  as in the fully reduced flavodoxins from C. beijerinckii and D. vulgaris.
5 observed in the flavodoxins from Clostridium beijerinckii and Desulfovibrio vulgaris.
6 eroides xylanisolvens ASCUSBF52, Clostridium beijerinckii ASCUSBF26, and Syntrophococcus sp. ASCUSBF6
7      Insertional inactivation of spo0A in C. beijerinckii blocked the formation of solvents (as well
8 d compared to the results of the Clostridium beijerinckii ( C. beijerinckii) flavodoxin.
9 hus far and we demonstrated that Clostridium beijerinckii can move via gliding motility.
10 ntly, an [FeFe] hydrogenase from Clostridium beijerinckii (CbHydA1) was reported to regain its cataly
11 face loop in the flavodoxin from Clostridium beijerinckii comprised of residues -Met(56)-Gly-Asp-Glu(
12 tosynthetic H(2) production by a Clostridium beijerinckii [FeFe]-hydrogenase (H(2)ase).
13 ormers, mostly O-down, exists in oxidized C. beijerinckii flavodoxin in the absence of intermolecular
14 urn -Met56-Gly-Asp-Glu59- in the Clostridium beijerinckii flavodoxin provides the majority of the cri
15                                    In the C. beijerinckii flavodoxin, the E sq/hq downshift because o
16 m that, in crystals of wild-type oxidized C. beijerinckii flavodoxin, the Gly57-Asp58 peptide adopts
17                           In the Clostridium beijerinckii flavodoxin, the reduction of the flavin mon
18 sing a thermodynamic scheme developed for C. beijerinckii flavodoxin.
19  low reduction potential exhibited by the C. beijerinckii flavodoxin.
20 in the D. vulgaris flavodoxin than in the C. beijerinckii flavodoxin.
21 mall, i.e., less than half of that in the C. beijerinckii flavodoxin.
22 results of the Clostridium beijerinckii ( C. beijerinckii) flavodoxin.
23                        In D. vulgaris and C. beijerinckii flavodoxins, the protein side chain causes
24 is couple in the flavodoxin from Clostridium beijerinckii has been attributed to the ionization of th
25          The FeFe hydrogenase of Clostridium beijerinckii is a very active catalyst of H(2) evolution
26 nase/reductase, respectively, in Clostridium beijerinckii NCIMB 8052 (Cb), resulting in two strains:
27               The spo0A genes of Clostridium beijerinckii NCIMB 8052 and Clostridium cellulolyticum A
28 ressions of 5168 genes capturing 98.6% of C. beijerinckii NCIMB 8052 genome were examed.
29 ty of >1 million variants of the Clostridium beijerinckii pfl ZTP riboswitch designed to perturb step
30 signal recognition particle RNA, Clostridium beijerinckii pfl ZTP riboswitch, and Bacillus cereus crc
31             By investigating the Clostridium beijerinckii pfl ZTP riboswitch, we identify multiple me
32 periments using C. acetobutylicum adc and C. beijerinckii ptb promoter fragments and recombinant Baci
33  (13)C-labeled green microalga Parachlorella beijerinckii reveal that starch is the most abundant pol
34 type and mutant flavodoxins from Clostridium beijerinckii show that the conformation of the peptide G
35 nts and recombinant Bacillus subtilis and C. beijerinckii Spo0A suggested that adc and ptb are direct
36                       Degenerate Clostridium beijerinckii strain (DG-8052) can be partially recovered
37           In the flavodoxin from Clostridium beijerinckii, the gamma-carboxylate group of glutamate-5
38           In the flavodoxin from Clostridium beijerinckii, the sulfur atom of methionine 56 is in dir
39 tolerant [FeFe] hydrogenase from Clostridium beijerinckii using a flexible [GGS](4) linker group (CbH
40 onally fused to the gusA reporter gene in C. beijerinckii validated this hypothesis.
41 mutant flavodoxins obtained from Clostridium beijerinckii were calculated by considering the protonat