Site-specific interaction between hydrocarbon cations and inert ligands: IR spectra of isomeric C3H3+–L dimers (L = Ne,Ar,O2,N2,CO2)

2002 ◽  
Vol 4 (20) ◽  
pp. 4855-4865 ◽  
Author(s):  
Doris Roth ◽  
Otto Dopfer

2015 ◽  
Vol 25 (4) ◽  
pp. 1063-1083 ◽  
Author(s):  
Jayaraman Jayabharathi ◽  
Periyasamy Ramanathan ◽  
Chockalingam Karunakaran ◽  
Venugopal Thanikachalam


2013 ◽  
Vol 135 (8) ◽  
pp. 2943-2946 ◽  
Author(s):  
Alexander S. Maltsev ◽  
Jue Chen ◽  
Rodney L. Levine ◽  
Ad Bax


2005 ◽  
Vol 187 (8) ◽  
pp. 2693-2697 ◽  
Author(s):  
Liliana Mora ◽  
Nancy Diaz ◽  
Richard H. Buckingham ◽  
Miklos de Zamaroczy

ABSTRACT The transfer RNase colicin D and ionophoric colicin B appropriate the outer membrane iron siderophore receptor FepA and share a common translocation requirement for the TonB pathway to cross the outer membrane. Despite the almost identical sequences of the N-terminal domains required for the translocation of colicins D and B, two spontaneous tonB mutations (Arg158Ser and Pro161Leu) completely abolished colicin D toxicity but did not affect either the sensitivity to other colicins or the FepA-dependent siderophore uptake capacity. The sensitivity to colicin D of both tonB mutants was fully restored by specific suppressor mutations in the TonB box of colicin D, at Ser18(Thr) and Met19(Ile), respectively. This demonstrates that the interaction of colicin D with TonB is critically dependent on certain residues close to position 160 in TonB and on the side chains of certain residues in the TonB box of colicin D. The effect of introducing the TonB boxes from other TonB-dependent receptors and colicins into colicins D and B was studied. The results of these and other changes in the two TonB boxes show that the role of residues at positions 18 and 19 in colicin D is strongly modulated by other nearby and/or distant residues and that the overall function of colicin D is much more dependent on the interaction with TonB involving the TonB box than is the function of colicin B.



2012 ◽  
Vol 116 (11) ◽  
pp. 3650-3658 ◽  
Author(s):  
Nataliya Popovych ◽  
Jeffrey R. Brender ◽  
Ronald Soong ◽  
Subramanian Vivekanandan ◽  
Kevin Hartman ◽  
...  


Biochemistry ◽  
1989 ◽  
Vol 28 (6) ◽  
pp. 2355-2359 ◽  
Author(s):  
Qiu Guo ◽  
Nadrian C. Seeman ◽  
Neville R. Kallenbach




1996 ◽  
Vol 24 (4) ◽  
pp. 512S-512S
Author(s):  
Dilara M. Isaeva




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