Publicação
Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases
| dc.contributor.author | Moura, José J. G. | |
| dc.contributor.author | Brondino, Carlos D. | |
| dc.contributor.author | Trincão, José | |
| dc.contributor.author | Romão, Maria J. | |
| dc.date.accessioned | 2013-02-06T12:11:30Z | |
| dc.date.available | 2013-02-06T12:11:30Z | |
| dc.date.issued | 2004 | |
| dc.description | J Biol Inorg Chem (2004) 9: 791–799 DOI 10.1007/s00775-004-0573-9 | por |
| dc.description.abstract | Molybdenum and tungsten are second- and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sulfite oxidase. The proteins of the DMSO reductase family present the widest diversity of properties among its members and our knowledge about this family was greatly broadened by the study of the enzymes nitrate reductase and formate dehydrogenase, obtained from different sources. We discuss in this review the information of the better characterized examples of these two types of Mo enzymes and W enzymes closely related to the members of the DMSO reductase family. We briefly summarize, also, the few cases reported so far for enzymes that can function either with Mo or W at their active site. | por |
| dc.identifier.issn | 0949-8257 | |
| dc.identifier.uri | http://hdl.handle.net/10362/8713 | |
| dc.language.iso | eng | por |
| dc.peerreviewed | yes | por |
| dc.publisher | Springer | por |
| dc.relation.publisherversion | http://link.springer.com/article/10.1007%2Fs00775-004-0573-9 | por |
| dc.subject | DMSO reductase family | por |
| dc.subject | Formate dehydrogenase | por |
| dc.subject | Molybdenum-containing enzymes | por |
| dc.subject | Nitrate reductase | por |
| dc.subject | Tungsten-containing enzymes | por |
| dc.title | Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases | por |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.citation.endPage | 799 | por |
| oaire.citation.startPage | 791 | por |
| oaire.citation.title | JBIC Journal of Biological Inorganic Chemistry | por |
| oaire.citation.volume | 9 | por |
| rcaap.rights | openAccess | por |
| rcaap.type | article | por |