Zobrazeno 1 - 10
of 11
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cad794a7534bbafaa1f6fa136fa310c3
https://pubmed.ncbi.nlm.nih.gov/35380039
https://pubmed.ncbi.nlm.nih.gov/35380039
Publikováno v:
Protein Science. 32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fcd5f76711afa5b28662752825a03573
https://doi.org/10.1002/pro.4615
https://doi.org/10.1002/pro.4615
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::420e072f4e7a2714f2e22da561e0e773
https://doi.org/10.1021/jacs.9b06988
https://doi.org/10.1021/jacs.9b06988
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aece85f0713ee7ff2e9a0c37ed47cc8b
https://doi.org/10.1021/acs.biochem.9b00312
https://doi.org/10.1021/acs.biochem.9b00312
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68b49f9fb4da3a08b6cb49c412c759be
https://doi.org/10.1016/j.jinorgbio.2022.111780
https://doi.org/10.1016/j.jinorgbio.2022.111780
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::45b547b5f834d10d8076c56268507d7c
https://doi.org/10.1002/pro.3491
https://doi.org/10.1002/pro.3491
Autor:
Ninian J. Blackburn, Renee J. Arias
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 77:a102-a102
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a218c10343e133ffb8984bdb2f6113aa
https://doi.org/10.1107/s0108767321098974
https://doi.org/10.1107/s0108767321098974
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3f841aff42b655ef68f81398b7af2035
https://pubmed.ncbi.nlm.nih.gov/30317480
https://pubmed.ncbi.nlm.nih.gov/30317480
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cd6717f676393b67ac3c94f4ba9cf17c
https://pubmed.ncbi.nlm.nih.gov/30056633
https://pubmed.ncbi.nlm.nih.gov/30056633