Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Chiara Rutanen"'
Autor:
Leena Penttinen, Chiara Rutanen, Markku Saloheimo, Kristiina Kruus, Juha Rouvinen, Nina Hakulinen
Publikováno v:
PLoS ONE, Vol 13, Iss 5, p e0196691 (2018)
Coupled binuclear copper (CBC) enzymes have a conserved type 3 copper site that binds molecular oxygen to oxidize various mono- and diphenolic compounds. In this study, we found a new crystal form of catechol oxidase from Aspergillus oryzae (AoCO4) a
Externí odkaz:
https://doaj.org/article/57e69b0feb694d14bee39c8a4c6bc899
Autor:
Anu, Hangas, Nina J, Kekäläinen, Alisa, Potter, Craig, Michell, Kauko J, Aho, Chiara, Rutanen, Johannes N, Spelbrink, Jaakko L, Pohjoismäki, Steffi, Goffart
Publikováno v:
Nucleic acids research. 50(15)
Mitochondrial DNA has been investigated for nearly fifty years, but many aspects of the maintenance of this essential small genome remain unknown. Like any genome, mammalian mitochondrial DNA requires the function of topoisomerases to counter and reg
Publikováno v:
Chembiochem : a European journal of chemical biology. 19(22)
Catechol oxidases and tyrosinases are coupled binuclear copper enzymes that oxidize various o-diphenolic compounds to corresponding o-quinones. Tyrosinases have an additional monooxygenation ability to hydroxylate monophenol to o-diphenol. It is stil
Autor:
Kristiina Kruus, Nina Hakulinen, Markku Saloheimo, Chiara Rutanen, Juha Rouvinen, Leena Penttinen
Publikováno v:
Penttinen, L, Rutanen, C, Saloheimo, M, Kruus, K, Rouvinen, J & Hakulinen, N 2018, ' A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes ', PLoS ONE, vol. 13, no. 5, e0196691 . https://doi.org/10.1371/journal.pone.0196691
'PloS One ', vol: 13, pages: e0196691-1-e0196691-15 (2018)
PLoS ONE
PLoS ONE, Vol 13, Iss 5, p e0196691 (2018)
'PloS One ', vol: 13, pages: e0196691-1-e0196691-15 (2018)
PLoS ONE
PLoS ONE, Vol 13, Iss 5, p e0196691 (2018)
Coupled binuclear copper (CBC) enzymes have a conserved type 3 copper site that binds molecular oxygen to oxidize various mono- and diphenolic compounds. In this study, we found a new crystal form of catechol oxidase from Aspergillus oryzae (AoCO4) a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e28104e007b228b7090ece585723b080
https://cris.vtt.fi/en/publications/f8fa10c8-1ba4-4927-87aa-8cbf4980b16b
https://cris.vtt.fi/en/publications/f8fa10c8-1ba4-4927-87aa-8cbf4980b16b