Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center

Biochemistry ◽  
1993 ◽  
Vol 32 (41) ◽  
pp. 11173-11180 ◽  
Author(s):  
Jeffrey W. Thomas ◽  
Laura J. Lemieux ◽  
James O. Alben ◽  
Robert B. Gennis
Keyword(s):  
Escherichia Coli ◽  
Transmembrane Helix ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Conserved Residues ◽  
Cytochrome Bo ◽  
Ubiquinol Oxidase ◽  
Binuclear Center

Site-Directed Mutagenesis of Residues within Helix VI in Subunit I of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli Suggests That Tyrosine 288 May Be a CuB Ligand

Biochemistry ◽  
1994 ◽  
Vol 33 (44) ◽  
pp. 13013-13021 ◽  
Author(s):  
Jeffrey W. Thomas ◽  
Melissa W. Calhoun ◽  
Laura J. Lemieux ◽  
Anne Puustinen ◽  
Marten Wikstrom ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ubiquinol Oxidase ◽  
Cytochrome Bo3

scholarly journals Site-Directed Mutagenesis Analysis of Amino Acids Critical for Activity of the Type I Signal Peptidase of the Archaeon Methanococcus voltae

2005 ◽  
Vol 187 (3) ◽  
pp. 1188-1191 ◽  
Author(s):  
Sonia L. Bardy ◽  
Sandy Y. M. Ng ◽  
David S. Carnegie ◽  
Ken F. Jarrell
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Aspartic Acid ◽  
Site Directed Mutagenesis ◽  
Signal Peptidase ◽  
Directed Mutagenesis ◽  
Type I ◽  
Aspartic Acid Residue ◽  
Conserved Residues ◽  
Methanococcus Voltae

ABSTRACT Site-directed mutagenesis studies of the signal peptidase of the methanogenic archaeon Methanococcus voltae identified three conserved residues (Ser52, His122, and Asp148) critical for activity. The requirement for one conserved aspartic acid residue distinguishes the archaeal enzyme from both the Escherichia coli and yeast Sec11 enzymes.

Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli

Biochemistry ◽  
1993 ◽  
Vol 32 (48) ◽  
pp. 13254-13261 ◽  
Author(s):  
Melissa W. Calhoun ◽  
Laura J. Lemieux ◽  
Jeffrey W. Thomas ◽  
John J. Hill ◽  
Visala Chepuri Goswitz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Spectroscopic Characterization ◽  
Axial Ligand ◽  
Cytochrome Bo ◽  
Ubiquinol Oxidase ◽  
Binuclear Center
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