The highly conserved methionine of subunit I of the heme-copper oxidases is not at the heme-copper dinuclear center: Mutagenesis of M110 in subunit I of cytochromebo3-type ubiquinol oxidase fromEscherichia coli
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00696-7/fullpdf
Reference26 articles.
1. Wikström M. Krab K. Saraste M. Cytochrome Oxidase - a Synthesis 1981 Academic Press New York, NY
2. The Binuclear Site of Cytochrome c Oxidase Structural Evidence from Iron X-ray Absorption Spectroscopy
3. Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis
4. A comparative review of the structure and function of cytochrome o from Escherichia coli and cytochrome aa3
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1. Identification of functionally conserved residues with the use of entropy-variability plots;Proteins: Structure, Function, and Bioinformatics;2003-07-31
2. Biogenesis of respiratory cytochromes in bacteria;Microbiology and Molecular Biology Reviews;1997-09
3. EPR studies of wild-type and several mutants of cytochromecoxidase fromRhodobacter sphaeroides: Glu286is not a bridging ligand in the cytochromea3-CuBcenter;FEBS Letters;1995-11-06
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