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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Huang, Yafei Lee, Hyun Ju Adelroth, Pia Reimann, Joachim |
| Description | Author Affiliation: Lee HJ ( Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.) |
| Abstract | Heme–copper oxidases (HCuOs) terminate the respiratory chain in mitochondria and most bacteria. They are transmembrane proteins that catalyse the reduction of oxygen and use the liberated free energy to maintain a proton-motive force across the membrane. The HCuO superfamily has been divided into the oxygen-reducing A-, B- and C-type oxidases as well as the bacterial NO reductases (NOR), catalysing the reduction of NO in the denitrification process. Proton transfer to the catalytic site in the mitochondrial-like A family occurs through two well-defined pathways termed the D- and K-pathways. The B, C, and NOR families differ in the pathways as well as the mechanisms for proton transfer to the active site and across the membrane. Recent structural and functional investigations, focussing on proton transfer in the B, C and NOR families will be discussed in this review. This article is part of a Special Issue entitled: Respiratory Oxidases. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1817 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Heme Metabolism Oxidoreductases Proton Pumps Protons Bacterial Proteins Chemistry Biological Transport Catalytic Domain Kinetics Models, Molecular Oxidation-Reduction Classification Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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