TY - JOUR
T1 - Oxidative phosphorylation in mutants of Escherichia coli defective in energy transduction
AU - Gutnick, D. L.
AU - Kanner, B. I.
AU - Postma, P. W.
PY - 1972/11/17
Y1 - 1972/11/17
N2 - Two mutants defective in oxidative phosphorylation have been isolated from Escherichia coli K12. The mutants lack ATP-driven transhydrogenase activity and exhibit P/NADH ratios, as measured in whole cells, of 0.04 and 0.16, respectively, as compared with a parental value of 2.1. Respiration-linked transhydrogenase was detected in membrane particles from the two strains. One of the mutants was defective in membrane (Mg2+-Ca2+-ATPase activity while the second strain exhibited a level of ATPase activity comparable to that in the parent. The ATPase in this latter mutant appeared to be converted to a form which is resistant to the inhibitor N,N′-dicyclohexylcarbodiimide.
AB - Two mutants defective in oxidative phosphorylation have been isolated from Escherichia coli K12. The mutants lack ATP-driven transhydrogenase activity and exhibit P/NADH ratios, as measured in whole cells, of 0.04 and 0.16, respectively, as compared with a parental value of 2.1. Respiration-linked transhydrogenase was detected in membrane particles from the two strains. One of the mutants was defective in membrane (Mg2+-Ca2+-ATPase activity while the second strain exhibited a level of ATPase activity comparable to that in the parent. The ATPase in this latter mutant appeared to be converted to a form which is resistant to the inhibitor N,N′-dicyclohexylcarbodiimide.
UR - http://www.scopus.com/inward/record.url?scp=0015514258&partnerID=8YFLogxK
U2 - 10.1016/0005-2728(72)90237-X
DO - 10.1016/0005-2728(72)90237-X
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C2 - 4145066
AN - SCOPUS:0015514258
SN - 0005-2728
VL - 283
SP - 217
EP - 222
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 2
ER -