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of 6
pro vyhledávání: '"Adrienne R. Diebold"'
Autor:
Christina D. Brown-Marshall, Adrienne R. Diebold, Michael L. Neidig, Graham R. Moran, Edward I. Solomon, June M. Brownlee
Publikováno v:
Journal of the American Chemical Society. 133:18148-18160
The α-keto acid-dependent dioxygenases are a major subgroup within the O(2)-activating mononuclear nonheme iron enzymes. For these enzymes, the resting ferrous, the substrate plus cofactor-bound ferrous, and the Fe(IV)═O states of the reaction hav
Autor:
Michael L. Neidig, Grit Daniela Straganz, Graham R. Moran, Edward I. Solomon, Adrienne R. Diebold
Publikováno v:
Biochemistry. 49:6945-6952
The oxygen activating mononuclear non-heme ferrous enzymes catalyze a diverse range of chemistry yet typically maintain a common structural motif: two histidines and a carboxylate coordinating the iron center in a facial triad. A new FeII coordinatin
Publikováno v:
Biochemistry. 49:1176-1182
Isopenicillin N synthase (IPNS) can have both oxidase and oxygenase activity depending on the substrate. For the native substrate, ACV, oxidase activity exists; however, for the substrate analogue ACOV, which lacks an amide nitrogen, IPNS exhibits ox
The O(2) activating mononuclear nonheme iron enzymes generally have a common facial triad (two histidine and one carboxylate (Asp or Glu) residue) ligating Fe(II) at the active site. Exceptions to this motif have recently been identified in nonheme e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87ead7e085570f07fb18c762d2764d2c
https://europepmc.org/articles/PMC3191879/
https://europepmc.org/articles/PMC3191879/
Autor:
Takehiko Tosha, Jennifer K. Schwartz, Adrienne R. Diebold, Elizabeth C. Theil, Edward I. Solomon, Xiaofeng S. Liu
Publikováno v:
Biochemistry. 49(49)
DNA protection during starvation (Dps) proteins are miniferritins found in bacteria and archaea that provide protection from uncontrolled Fe(II)/O radical chemistry; thus the catalytic sites are targets for antibiotics against pathogens, such as anth
Publikováno v:
Biochemistry. 49(5)
Diketone cleaving enzyme (Dke1) is a dioxygenase with an atypical, three-histidine-ligated, mononuclear non-heme Fe(2+) center. To assess the role in enzyme catalysis of the hydrophilic residues in the active site pocket, residues Glu98, Arg80, Tyr70