Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Nazmiye Erdin"'
Autor:
Nazmiye Erdin, Klaus-Dieter Müller, Thomas Gaudszun, Iradj Amiri, Joachim Vater, Johann Salnikow
Publikováno v:
Advances in Photosynthesis Research ISBN: 9789024729449
Ribulose 1,5-bisphosphate carboxylase/oxygenase (MW ca. 550,000) is a bifunctional enzyme responsible for photosynthetic carbon dioxide fixation as well as oxygenolytic scission of the pentose substrate initiating the process of photorespiration. Car
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::299e86bbf6adefbd497a6558cace6e5b
https://doi.org/10.1007/978-94-017-4973-2_180
https://doi.org/10.1007/978-94-017-4973-2_180
Catalysis and regulation of CO2 fixation differ in a characteristic manner in their response to anionic modifiers and the polarity of the reaction medium. Monovalent inorganic anions inhibit catalysis and CO2-activation of the ᴅ-ribulose 1,5-bispho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f951a71ebb4799c0abbc52d64dab3b0
Publikováno v:
Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie. 27(9)
4-hydroxybenzoate hydroxylase from Ps. putida has been studied with regard to the oxygen interaction with the reduced flavin. By rapid scanning spectrophotometry and EPR-measurements of rapidly frozen mixtures no intermediate could be established eit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49995172ddfaa333830d3c50445b7ad0
https://pubmed.ncbi.nlm.nih.gov/4405079
https://pubmed.ncbi.nlm.nih.gov/4405079
Publikováno v:
European journal of biochemistry. 35(1)
The interaction of substrates with a 4-methoxybenzoate O-demethylating enzyme system was studied by use of crude cell-free extracts and also by the purified enzyme system. The two components of the enzyme system, an iron-containing flavoprotein and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eee4efd0f4dc5456c0da1621e9b4ed6a
https://pubmed.ncbi.nlm.nih.gov/4351526
https://pubmed.ncbi.nlm.nih.gov/4351526