Back to Search
Start Over
The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping.
- Source :
-
Science . 7/16/2010, Vol. 329 Issue 5989, p327-330. 4p. - Publication Year :
- 2010
-
Abstract
- The heme-copper oxidases (HCOs) accomplish the key event of aerobic respiration; they couple O2 reduction and transmembrane proton pumping. To gain new insights into the still enigmatic process, we structurally characterized a C-family HCO—essential for the pathogenicity of many bacteria—that differs from the two other HCO families, A and B, that have been structurally analyzed. The x-ray structure of the C-family cbb3 oxidase from Pseudomonas stutzeri at 3.2 angstrom resolution shows an electron supply system different from families A and B. Like family-B HCOs, C HCOs have only one pathway, which conducts protons via an alternative tyrosine-histidine cross-link. Structural differences around hemes b and b3 suggest a different redox-driven proton-pumping mechanism and provide clues to explain the higher activity of family-C HCOs at low oxygen concentrations. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00368075
- Volume :
- 329
- Issue :
- 5989
- Database :
- Academic Search Index
- Journal :
- Science
- Publication Type :
- Academic Journal
- Accession number :
- 52621747
- Full Text :
- https://doi.org/10.1126/science.1187303