Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in Escherichia coli K12

1996 ◽  
Vol 253 (1-2) ◽  
pp. 95-102 ◽  
Author(s):  
R. Metheringham ◽  
K. L. Tyson ◽  
H. Crooke ◽  
D. Missiakas ◽  
S. Raina ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Electron Transfer ◽  
Bond Formation ◽  
Disulphide Bond ◽  
Escherichia Coli K12 ◽  
Disulphide Bond Formation

scholarly journals Chemical modification of Escherichia coli succinyl-CoA synthetase with the adenine nucleotide analogue 5′-p-fluorosulphonylbenzoyladenosine

1983 ◽  
Vol 215 (3) ◽  
pp. 513-518 ◽  
Author(s):  
A R S Prasad ◽  
J Ybarra ◽  
J S Nishimura
Keyword(s):  
Escherichia Coli ◽  
Catalytic Activity ◽  
Adenine Nucleotide ◽  
Bond Formation ◽  
Disulphide Bond ◽  
Thiol Groups ◽  
Binding Region ◽  
Nucleotide Analogue ◽  
Disulphide Bond Formation ◽  
Succinyl Coa Synthetase

Escherichia coli succinyl-CoA synthetase (EC 6.2.1.5) was irreversibly inactivated on incubation with the adenine nucleotide analogue 5′-p-fluorosulphonylbenzoyladenosine (5′-FSBA). Optimal inactivation by 5′-FSBA took place in 40% (v/v) dimethylformamide. ATP and ADP protected the enzyme against inactivation by 5′-FSBA, whereas desulpho-CoA, an analogue of CoA, did not. Inactivation of succinyl-CoA synthetase by 5′-FSBA resulted in total loss of almost four thiol groups per alpha beta-dimer, of which two groups appeared to be essential for catalytic activity. 5′-FSBA at the first instance appeared to interact non-specifically with non-essential thiol groups, followed by a more specific reaction with essential thiol groups in the ATP(ADP)-binding region. Plots of the data according to the method of Tsou [(1962) Sci. Sin. 11, 1535-1558] revealed that, of the two slower-reacting thiol groups, only one was essential for catalytic activity. When succinyl-CoA synthetase that had been totally inactivated by 5′-FSBA was unfolded in acidic urea and then refolded in the presence of 100 mM-dithiothreitol, 85% of the activity, in comparison with the appropriate control, was restored. These data are interpreted to indicate that inactivation of succinyl-CoA synthetase by 5′-FSBA involves the formation of a disulphide bond between two cysteine residues. Disulphide bond formation likely proceeds via a thiosulphonate intermediate between 5′-p-sulphonylbenzoyladenosine and one of the reactive thiol groups of the enzyme.

Crystallization of DsbA, an Escherichia coli Protein Required for Disulphide Bond Formation in Vivo

1993 ◽  
Vol 230 (3) ◽  
pp. 1097-1100 ◽  
Author(s):  
Jennifer L. Martin ◽  
Gabriel Waksman ◽  
James C.A. Bardwell ◽  
Jon Beckwith ◽  
John Kuriyan
Keyword(s):  
Escherichia Coli ◽  
Bond Formation ◽  
Disulphide Bond ◽  
Disulphide Bond Formation

Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation

1995 ◽  
Vol 17 (6) ◽  
pp. 1035-1044 ◽  
Author(s):  
Kim R. Hardie ◽  
Angela Schulze ◽  
Michael W. Parker ◽  
J. Thomas Buckley
Keyword(s):  
Bond Formation ◽  
Disulphide Bond ◽  
Disulphide Bond Formation ◽  
Vibrio Spp

scholarly journals A Mutant Defective in Electron Transfer to Nitrate in Escherichia coli K12

Microbiology ◽  
1980 ◽  
Vol 117 (1) ◽  
pp. 257-262
Author(s):  
V. Orth ◽  
M. Chippaux ◽  
M.-C. Pascal
Keyword(s):  
Escherichia Coli ◽  
Electron Transfer ◽  
Escherichia Coli K12
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