Electrostatic Effects of Surface Acidic Amino Acid Residues on the Oxidation-Reduction Potentials of the Flavodoxin from Desulfovibrio vulgaris (Hildenborough)

Biochemistry ◽  
1995 ◽  
Vol 34 (10) ◽  
pp. 3183-3192 ◽  
Author(s):  
Zhimin Zhou ◽  
Richard P. Swenson
ChemBioChem ◽  
2015 ◽  
Vol 16 (14) ◽  
pp. 2080-2085 ◽  
Author(s):  
Sébastien Kriegel ◽  
Batoul Srour ◽  
Stefan Steimle ◽  
Thorsten Friedrich ◽  
Petra Hellwig

2005 ◽  
Vol 4 (6) ◽  
pp. 1057-1065 ◽  
Author(s):  
M. Wilhelm ◽  
F.-X. Wilhelm

ABSTRACT Reverse transcriptase (RT) with its associated RNase H (RH) domain and integrase (IN) are key enzymes encoded by retroviruses and retrotransposons. Several studies have implied a functional role of the interaction between IN and RT during the replication of retroviral and retrotransposon genomes. In this study, IN deletion mutants were used to investigate the role of IN on the RT activity of the yeast Saccharomyces cerevisiae retrotransposon Ty1. We have identified two domains of Ty1 integrase which have effects on RT activity in vivo. The deletion of a domain spanning amino acid residues 233 to 520 of IN increases the exogenous specific activity of RT up to 20-fold, whereas the removal of a region rich in acidic amino acid residues between residues 521 and 607 decreases its activity. The last result complements our observation that an active recombinant RT protein can be obtained if a small acidic tail mimicking the acidic domain of IN is fused to the RT-RH domain. We suggest that interaction between these acidic amino acid residues of IN and a basic region of RT could be critical for the correct folding of RT and for the formation of an active conformation of the enzyme.


1971 ◽  
Vol 49 (6) ◽  
pp. 641-646 ◽  
Author(s):  
M. V. Laycock ◽  
J. S. Craigie

Cytochrome 553, an electron carrier in photosynthesis and a functional analogue of cytochrome f of higher plants, was isolated from Monochrysis lutheri and purified by salt fractionation, chromatography, and isoelectric focussing. Absorption maxima occurred at 275, 320, 416, 523, and 553 nm in the reduced form. The α-absorption peak was symmetrical and had an extinction coefficient of 25.9 mM−1 cm−1. The molecular weight was 11 100 by equilibrium centrifugation, 12 400 from iron determinations, and 10 300 from the amino acid composition. The molecule consisted of one heme group and 91 amino acid residues including two cysteine residues and one each of histidine, arginine, tryptophan, methionine, and proline. Other physical properties measured were: the sedimentation coefficient, 1.3 S; the normal oxidation reduction potential, + 0.388 V; and the isoelectric point, pH 3.75.


PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e52776 ◽  
Author(s):  
Akemi Shodai ◽  
Akemi Ido ◽  
Noriko Fujiwara ◽  
Takashi Ayaki ◽  
Toshifumi Morimura ◽  
...  

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