Structure and function of electron transport systems

1971 ◽  
Vol 76 (2) ◽  
pp. 174-182 ◽  
Author(s):  
M. Boll
Keyword(s):  
Electron Transport ◽  
Structure And Function ◽  
Transport Systems ◽  
And Function

scholarly journals CHLOROPLAST STRUCTURE AND FUNCTION IN ac-20, A MUTANT STRAIN OF CHLAMYDOMONAS REINHARDI

1970 ◽  
Vol 44 (3) ◽  
pp. 540-546 ◽  
Author(s):  
R. P. Levine ◽  
A. Paszewski
Keyword(s):  
Electron Transport ◽  
Mutant Strain ◽  
Electron Transport Chain ◽  
Co2 Fixation ◽  
Photosynthetic Electron Transport ◽  
Structure And Function ◽  
Wild Type ◽  
Carboxylase Activity ◽  
Transport Chain ◽  
And Function

Photosynthetic electron transport is markedly affected in mixotrophic cells of ac-20 because they lack the capacity to form the wild-type level of cytochrome 559, as well as Q, the quencher of fluorescence of photochemical system II. The other components of the electron-transport chain, as well as reactions dependent upon photochemical system I, are unaffected in the mutant strain. These observations are discussed in terms of the previously reported effects of the ac-20 mutation on CO2 fixation and ribulose-1,5-diphosphate carboxylase activity.

Structure and Function of Renal Organic Cation Transporters

Physiology ◽  
1998 ◽  
Vol 13 (1) ◽  
pp. 11-16 ◽  
Author(s):  
Hermann Koepsell ◽  
Andreas Busch ◽  
Valentin Gorboulev ◽  
Petra Arndt
Keyword(s):  
Plasma Membranes ◽  
Organic Cation ◽  
Structure And Function ◽  
Transport Systems ◽  
Organic Cations ◽  
Renal Tubules ◽  
Organic Cation Transporters ◽  
Cation Transporters ◽  
And Function

Polyspecific transport systems in the kidney mediate the excretion and reabsorption of organic cations. Electrogenic import systems and electroneutral export systems in the basolateral and luminal plasma membranes of proximal renal tubules are involved. Two subtypes of electrogenic import systems have been cloned from rats and humans and functionally characterized.

scholarly journals An Amino Acid Substitution in the QB-Protein Causes Herbicide Resistance without Impairing Electron Transport from QA to QB

1989 ◽  
Vol 44 (5-6) ◽  
pp. 431-434 ◽  
Author(s):  
Günter F. Wildner ◽  
Ursula Heisterkamp ◽  
Ulrich Bodner ◽  
Udo Johanmngmeier ◽  
Wolfgang Haehnel
Keyword(s):  
Amino Acid ◽  
Electron Transport ◽  
Sequence Analysis ◽  
Herbicide Resistance ◽  
Resistant Mutant ◽  
Structure And Function ◽  
Wild Type ◽  
Chlamydomonas Reinhardii ◽  
And Function ◽  
Kinetics Of

Abstract Structure and function of the QB-protein of a metribuzin resistant mutant of Chlamydomonas reinhardii were analyzed. The amino acid residue Leu-275 of the wild type protein is changed to Phe as was determined by RNA -sequence analysis. This mutation caused a 20-fold and 5-fold resistance to metribuzin and DCMU , respectively. No resistance to atrazine was observed. The kinetics of the electron transport from QA to OB was similar to that of the wild type (t1/2 = 0.4 ms).

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