Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Brent S. Rivard"'
Publikováno v:
Biochemistry. 56:4940-4950
CmlI catalyzes the six-electron oxidation of an aryl-amine precursor (NH2-CAM) to the aryl-nitro group of chloramphenicol (CAM). The active site of CmlI contains a (hydr)oxo- and carboxylate-bridged dinuclear iron cluster. During catalysis, a novel d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b33643147e600670055f7627af982cec
https://doi.org/10.1021/acs.biochem.7b00695
https://doi.org/10.1021/acs.biochem.7b00695
Autor:
Brent S. Rivard, Kiyoung Park, Shinji Kitao, Michael Hu, Jiyong Zhao, Martin Srnec, Makina Saito, Lei V. Liu, Makoto Seto, Melanie S. Rogers, Edward I. Solomon, Yasuhiro Kobayashi, Yoshitaka Yoda, Lars H. Böttger, John D. Lipscomb, Kyle D. Sutherlin
The Rieske dioxygenases are a major subclass of mononuclear nonheme iron enzymes that play an important role in bioremediation. Recently, a high-spin FeIII–(hydro)-peroxy intermediate (BZDOp) has been trapped in the peroxide shunt reaction of benzo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4695a1d11fdb8648cccdad435cde591
https://europepmc.org/articles/PMC5973823/
https://europepmc.org/articles/PMC5973823/
Autor:
Christopher J. Cramer, Sarmistha Chakrabarty, Melanie S. Rogers, John D. Lipscomb, Matthew B. Neibergall, Daniel J. Marell, Brent S. Rivard
Publikováno v:
Biochemistry. 54:4652-4664
Rieske dearomatizing dioxygenases utilize a Rieske iron-sulfur cluster and a mononuclear Fe(II) located 15 Å across a subunit boundary to catalyze O2-dependent formation of cis-dihydrodiol products from aromatic substrates. During catalysis, O2 bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0f768f6faf925eaae2371e1af2beb62
https://doi.org/10.1021/acs.biochem.5b00573
https://doi.org/10.1021/acs.biochem.5b00573
Publikováno v:
Journal of the American Chemical Society. 138(23)
The ultimate step in chloramphenicol (CAM) biosynthesis is a six-electron oxidation of an aryl-amine precursor (NH2-CAM) to the aryl-nitro group of CAM catalyzed by the non-heme diiron cluster-containing oxygenase CmlI. Upon exposure of the diferrous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d595bfb15dd7d2a642eab3bc20b25abe
https://pubmed.ncbi.nlm.nih.gov/27203126
https://pubmed.ncbi.nlm.nih.gov/27203126
Autor:
Lawrence Que, John D. Lipscomb, Katlyn K. Meier, Eckard Münck, Anna J. Komor, Brent S. Rivard, Van V. Vu, Thomas M. Makris
Streptomyces venezuelae CmlI catalyzes the six-electron oxygenation of the arylamine precursor of chloramphenicol in a nonribosomal peptide synthetase (NRPS)-based pathway to yield the nitroaryl group of the antibiotic. Optical, EPR, and Mössbauer s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46bb11d57dea66d66589eabb495bb959
https://europepmc.org/articles/PMC4318726/
https://europepmc.org/articles/PMC4318726/