Výsledky vyhledávání - "Evan F. Welch"

Pre-Steady-State Reactivity of Peptidylglycine Monooxygenase Implicates Ascorbate in Substrate Triggering of the Active Conformer

Autor: Evan F. Welch, Katherine W. Rush, Renee J. Arias, Ninian J. Blackburn

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

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New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism

Autor: Renee J. Arias, Evan F. Welch, Ninian J. Blackburn

Publikováno v: Protein Science. 32

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fcd5f76711afa5b28662752825a03573
https://doi.org/10.1002/pro.4615

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Catalytic M Center of Copper Monooxygenases Probed by Rational Design. Effects of Selenomethionine and Histidine Substitution on Structure and Reactivity

Autor: Katherine B. Alwan, Evan F. Welch, Ninian J. Blackburn

Publikováno v: Biochemistry

The M-centers of the mononuclear monooxygenases peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) bind and activate dioxygen on route to substrate hydroxylation. Recently we reported the rational design of a protein-based model

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44136fc819bee6b4e585eba1a5004db
https://doi.org/10.1021/acs.biochem.9b00823

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Rational Design of a Histidine–Methionine Site Modeling the M-Center of Copper Monooxygenases in a Small Metallochaperone Scaffold

Autor: Katherine B. Alwan, Renee J. Arias, Ninian J. Blackburn, Evan F. Welch, Ben F. Gambill

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

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Copper monooxygenase reactivity: Do consensus mechanisms accurately reflect experimental observations?

Autor: Evan F, Welch, Katherine W, Rush, Renee J, Arias, Ninian J, Blackburn

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

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