Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Renee J, Arias"'
Publikováno v:
Biochemistry. 61(8)
Peptidylglycine monooxygenase (PHM) is essential for the posttranslational amidation of neuroendocrine peptides. An important aspect of the PHM mechanism is the complete coupling of oxygen reduction to substrate hydroxylation, which implies no oxygen
Publikováno v:
Protein Science. 32
Autor:
Serena DeBeer, Douglas C. Rees, Dimosthenis Sokaras, Sergey Koroidov, Renee J. Arias, Thomas Kroll, Uwe Bergmann, Justin T. Henthorn
Publikováno v:
Journal of the American Chemical Society
The size and complexity of Mo-dependent nitrogenase, a multicomponent enzyme capable of reducing dinitrogen to ammonia, have made a detailed understanding of the FeMo cofactor (FeMoco) active site electronic structure an ongoing challenge. Selective
Publikováno v:
Biochemistry
Mononuclear copper monooxygenases peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) catalyze the hydroxylation of high energy C-H bonds utilizing a pair of chemically distinct copper sites (CuH and CuM) separated by 11 A. In ear
Publikováno v:
J Inorg Biochem
An important question is whether consensus mechanisms for copper monooxygenase enzymes such as peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) generated via computational and spectroscopic approaches account for important expe
Publikováno v:
Protein Science. 27:1837-1841
A simple "diffusion-to-capture" model is used to estimate the upper limit to the growth rate of macromolecular crystals under conditions when the rate limiting process is the mass transfer of sample from solution to the crystal. Under diffusion-limit
Autor:
Ninian J. Blackburn, Renee J. Arias
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 77:a102-a102
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1876
Nitrogenase is the only known enzymatic system capable of reducing atmospheric dinitrogen to ammonia. This unique reaction requires tightly choreographed interactions between the nitrogenase component proteins, the molybdenum-iron (MoFe)- and iron (F
Publikováno v:
Methods in Molecular Biology ISBN: 9781493988631
Nitrogenase is the only known enzymatic system capable of reducing atmospheric dinitrogen to ammonia. This unique reaction requires tightly choreographed interactions between the nitrogenase component proteins, the molybdenum-iron (MoFe)- and iron (F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b743a92e9a1eab3879ddbd6217cdc6c4
https://doi.org/10.1007/978-1-4939-8864-8_10
https://doi.org/10.1007/978-1-4939-8864-8_10
Publikováno v:
Protein Science : A Publication of the Protein Society
A simple “diffusion‐to‐capture” model is used to estimate the upper limit to the growth rate of macromolecular crystals under conditions when the rate limiting process is the mass transfer of sample from solution to the crystal. Under diffusi