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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lobo, Susana A. L. Carita, João N. Almeida, Claúdia C. Teixeira, Miguel Saraiva, Lígia M. |
| Description | Author Affiliation: Lobo SA ( Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República (EAN), 2780-157 Oeiras, Portugal.) |
| Abstract | The genome of the sulphate reducing bacterium Desulfovibrio vulgaris Hildenborough, still considered a strict anaerobe, encodes two oxygen reductases of the bd and haem–copper types. The haem–copper oxygen reductase deduced amino acid sequence reveals that it is a Type A2 enzyme, which in its subunit II contains two c -type haem binding motifs. We have characterized the cytochrome c domain of subunit II and confirmed the binding of two haem groups, both with Met-His iron coordination. Hence, this enzyme constitutes the first example of a $ccaa_{3}$ haem–copper oxygen reductase. The expression of D. vulgaris haem–copper oxygen reductase was found to be independent of the electron donor and acceptor source and is not altered by stress factors such as oxygen exposure, nitrite, nitrate, and iron; therefore the haem–copper oxygen reductase seems to be constitutive. The KCN sensitive oxygen reduction by D. vulgaris membranes demonstrated in this work indicates the presence of an active haem–copper oxygen reductase. D. vulgaris membranes perform oxygen reduction when accepting electrons from the monohaem cytochrome $c_{553}$ , thus revealing the first possible electron donor to the terminal oxygen reductase of D. vulgaris . The physiological implication of the presence of the oxygen reductase in this organism is discussed. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 12 |
| Volume Number | 1777 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2008-12-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Copper Metabolism Cytochromes c Chemistry Desulfovibrio Vulgaris Enzymology Heme Oxidoreductases Oxygen Protein Subunits Amino Acid Sequence Cell Membrane Cytochrome c Group Cytology Genetics Electrons Molecular Sequence Data Multigene Family Protein Structure, Tertiary Sequence Alignment Sequence Analysis, Protein Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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