Výsledky vyhledávání - "Irene Y. Kung"

Geometries and Electronic Structures of Cyanide Adducts of the Non-Heme Iron Active Site of Superoxide Reductases: Vibrational and ENDOR Studies

Autor: Francis E. Jenney, Christopher A. Cosper, Michael D. Clay, Michael K. Johnson, Rangan Krishnan, Tran Chin Yang, Brian M. Hoffman, Donald M. Kurtz, Michael W. W. Adams, Irene Y. Kung

Publikováno v: Biochemistry. 45:427-438

We have added cyanide to oxidized 1Fe and 2Fe superoxide reductase (SOR) as a surrogate for the putative ferric-(hydro)peroxo intermediate in the reaction of the enzymes with superoxide and have used vibrational and ENDOR spectroscopies to study the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df472c04e6fdec183da75b8880955c8d
https://doi.org/10.1021/bi052034v

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Structural Comparison of Five-Coordinate Thiolate-Ligated MII = FeII, CoII, NiII, and ZnII Ions Wrapped in a Chiral Helical Ligand

Autor: Jeffrey J. Ellison, Irene Y. Kung, Andrew M. Nienstedt, Steven C. Shoner, Julie A. Kovacs, David M. Barnhart

Publikováno v: Inorganic Chemistry. 37:5721-5726

The syntheses and structures of two analogous five-coordinate mixed nitrogen/thiolate-ligated Co2+ and Fe2+ complexes are described and compared to their previously reported Zn2+ and Ni2+ analogues...

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d8bff3cc73b5a214cc895c7befff16ae
https://doi.org/10.1021/ic980882r

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EPR and ENDOR evidence for a 1-His, hydroxo-bridged mixed-valent diiron site in Desulfovibrio vulgaris rubrerythrin

Autor: Brian M. Hoffman, Donald M. Kurtz, Stoyan K. Smoukov, Peter E. Doan, Bradley E. Sturgeon, Irene Y. Kung, Roman Davydov

Publikováno v: Biochemistry. 42(20)

Key features differentiating the coordination environment of the two irons in the mixed-valent (Fe(2+),Fe(3+)) diiron site of Desulfovibrio vulgaris rubrerythrin (Rbr(mv)) were determined by continuous wave (CW) and pulsed ENDOR spectroscopy at 35GHz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9d9f09212fdf6b315a54130acccb159
https://pubmed.ncbi.nlm.nih.gov/12755623

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Why Is There an 'Inert' Metal Center in the Active Site of Nitrile Hydratase? Reactivity and Ligand Dissociation from a Five-Coordinate Co(III) Nitrile Hydratase Model

Autor: Irene Y. Kung, Jason Shearer, Julie A. Kovacs, Werner Kaminsky, Scott Lovell

To determine how a substitutionally inert metal can play a catalytic role in the metalloenzyme nitrile hydratase (NHase), a reactive five-coordinate Co(III) thiolate complex ([Co(III)(S(2)(Me2)N(3)(Pr,Pr))](PF(6)) (1)) that resembles the active site

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05e2797d4ed0c01b8227b792a56adc03
https://europepmc.org/articles/PMC4484831/

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A Co(III) Complex in a Mixed Sulfur/Nitrogen Ligand Environment: Modeling the Substrate- and Product-Bound Forms of the Metalloenzyme Thiocyanate Hydrolase

Autor: Jason Shearer, Irene Y. Kung, Julie A. Kovacs, Scott Lovell

Publikováno v: Inorganic Chemistry. 39:4998-4999

Thiocyanate hydrolase (TCH) is a pink bacterial metalloenzyme found in Thiobacillus thioparus THI 115 that catalyzes the conversion of thiocyanate to carbonyl sulfide and ammonia.1,2 Although TCH has not been well characterized spectroscopically, an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d23648f8d9118a9b1c20a6f56377ff6
https://doi.org/10.1021/ic0005689

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