Changes in the Reaction Mechanism of Electron Transfer from Plastocyanin to Photosystem I in the CyanobacteriumSynechocystissp. PCC 6803 As Induced by Site-Directed Mutagenesis of the Copper Protein†

Biochemistry ◽  
1997 ◽  
Vol 36 (33) ◽  
pp. 10125-10130 ◽  
Author(s):  
Berta De la Cerda ◽  
José A. Navarro ◽  
Manuel Hervás ◽  
Miguel A. De la Rosa
Keyword(s):  
Electron Transfer ◽  
Reaction Mechanism ◽  
Photosystem I ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Copper Protein ◽  
Pcc 6803

scholarly journals Site-directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus

1992 ◽  
Vol 288 (1) ◽  
pp. 117-121 ◽  
Author(s):  
E P Ko ◽  
H Akatsuka ◽  
H Moriyama ◽  
A Shinmyo ◽  
Y Hata ◽  
...  
Keyword(s):  
Amino Acids ◽  
Reaction Mechanism ◽  
Amino Acid ◽  
Bacillus Pumilus ◽  
Specific Activity ◽  
Sequence Similarity ◽  
Site Directed Mutagenesis ◽  
Dimensional Structure ◽  
Amino Acid Sequence Similarity ◽  
Directed Mutagenesis

To elucidate the reaction mechanism of xylanase, the identification of amino acids essential for its catalysis is of importance. Studies have indicated the possibility that the reaction mechanism of xylanase is similar to that of hen's egg lysozyme, which involves acidic amino acid residues. On the basis of this assumption, together with the three-dimensional structure of Bacillus pumilus xylanase and its amino acid sequence similarity to other xylanases of different origins, three acidic amino acids, namely Asp-21, Glu-93 and Glu-182, were selected for site-directed mutagenesis. The Asp residue was altered to either Ser or Glu, and the Glu residues to Ser or Asp. The purified mutant xylanases D21E, D21S, E93D, E93S, E182D and E182S showed single protein bands of about 26 kDa on SDS/PAGE. C.d. spectra of these mutant enzymes show no effect on the secondary structure of xylanase, except that of D21E, which shows a little variation. Furthermore, mutations of Glu-93 and Glu-182 resulted in a drastic decrease in the specific activity of xylanase as compared with mutation of Asp-21. On the basis of these results we propose that Glu-93 and Glu-182 are the best candidates for the essential catalytic residues of xylanase.

Enhanced Electron Transfer and Lauric Acid Hydroxylation by Site-Directed Mutagenesis of CYP119

2002 ◽  
Vol 124 (20) ◽  
pp. 5684-5691 ◽  
Author(s):  
Laura S. Koo ◽  
Chad E. Immoos ◽  
Michael S. Cohen ◽  
Patrick J. Farmer ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Electron Transfer ◽  
Lauric Acid ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Acid Hydroxylation

Site-directed mutagenesis reveals that the hydrophobic patch of azurin mediates electron transfer

1990 ◽  
Vol 112 (2) ◽  
pp. 907-908 ◽  
Author(s):  
Mart Van de Kamp ◽  
Rene Floris ◽  
Frits C. Hali ◽  
Gerard W. Canters
Keyword(s):  
Electron Transfer ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Hydrophobic Patch

scholarly journals Insights into the reaction mechanism of Escherichia coli agmatinase by site-directed mutagenesis and molecular modelling

2002 ◽  
Vol 269 (22) ◽  
pp. 5522-5526 ◽  
Author(s):  
Mónica Salas ◽  
Rolando Rodríguez ◽  
Nelia López ◽  
Elena Uribe ◽  
Vasthi López ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Reaction Mechanism ◽  
Molecular Modelling ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Importance of the Conserved Lysine 83 Residue ofZea maysCytochromeb561for Ascorbate-Specific Transmembrane Electron Transfer As Revealed by Site-Directed Mutagenesis Studies

Biochemistry ◽  
2009 ◽  
Vol 48 (44) ◽  
pp. 10665-10678 ◽  
Author(s):  
Nobuyuki Nakanishi ◽  
Motiur Md. Rahman ◽  
Yoichi Sakamoto ◽  
Tadakazu Takigami ◽  
Kazuo Kobayashi ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis
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