Zobrazeno 21 - 30
of 44
pro vyhledávání: '"35"'
Autor:
Georgieva ER; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA., Ramlall TF, Borbat PP, Freed JH, Eliezer D
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2008 Oct 01; Vol. 130 (39), pp. 12856-7. Date of Electronic Publication: 2008 Sep 06.
Autor:
Kay CW; Department of Biology, University College London, UK. c.kay@ucl.ac.uk, El Mkami H, Molla G, Pollegioni L, Ramsay RR
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2007 Dec 26; Vol. 129 (51), pp. 16091-7. Date of Electronic Publication: 2007 Nov 29.
Autor:
Schiemann O; Institut für Physikalische und Theoretische Chemie, J. W. Goethe-Universität, Marie-Curie-Strasse 11, 60439 Frankfurt am Main, Germany. o.schiemann@prisner.de, Weber A, Edwards TE, Prisner TF, Sigurdsson ST
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2003 Mar 26; Vol. 125 (12), pp. 3434-5.
Publikováno v:
J Am Chem Soc
We report an air-stable diradical dication of chiral D(2)-symmetric conjoined bis[5]diazahelicene with unprecedented high spin (triplet) ground state, singlet triplet energy gap, ΔE(ST) = 0.3 kcal mol(−1). The diradical dication possesses closed-s
Autor:
Petra Hänzelmann, Sowmya Subramanian, Michael K. Johnson, Brian M. Hoffman, Heather L. Hernandez, Hermann Schindelin, Nicholas S. Lees
Publikováno v:
Journal of the American Chemical Society. 131:9184-9185
The S-adenosylmethionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of guanosine 5'-triphosphate (5'-GTP) into precursor Z. A published X-ray crystal structure of MoaA wit
Autor:
Jeremy M. Smith, Brian M. Hoffman, Martin L. Kirk, Benjamin W. Stein, Deepak Subedi, George E. Cutsail
Publikováno v:
Journal of the American Chemical Society
The recently synthesized and isolated low-coordinate Fe(V) nitride complex has numerous implications as a model for high-oxidation states in biological and industrial systems. The trigonal [PhB((t)BuIm)3Fe(V)≡N](+) (where (PhB((t)BuIm)3(-) = phenyl
Autor:
Brian M. Hoffman, Joshua Telser, Brett M. Barney, Peter E. Doan, Lance C. Seefeldt, Robert Y. Igarashi, Dennis R. Dean
Publikováno v:
Journal of the American Chemical Society. 133:17329-17340
N(2) binds to the active-site metal cluster in the nitrogenase MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-homocitrate-X]; FeMo-co) only after the MoFe protein has accumulated three or four electrons/protons (E(3) or E(4) states), with the E(4) state
Autor:
Mohammad R. Seyedsayamdost, Tomislav Argirević, JoAnne Stubbe, Ellen Catherine Minnihan, Marina Bennati
Publikováno v:
Journal of the American Chemical Society
E. coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides, a process that requires long-range radical transfer over 35 A from a tyrosyl radical (Y(122)*) within the beta2 subunit to a cysteine residue (C(439))
Autor:
Peter E. Doan, Patricia C. Dos Santos, Hong-In Lee, Mikhail Laryukhin, Brian M. Hoffman, Lance C. Seefeldt, Dennis R. Dean, Robert Y. Igarashi
Publikováno v:
Journal of the American Chemical Society. 126:9563-9569
Nitrogenase is the metalloenzyme that catalyzes the nucleotide-dependent reduction of N(2), as well as reduction of a variety of other triply bonded substrates, including the alkyne, acetylene. Substitution of the alpha-70(Val) residue in the nitroge
Autor:
Koichiro Ishimori, Isao Morishima, Takehiko Tosha, Shiro Yoshioka, Hiroshi Hori, Satoshi Takahashi
Publikováno v:
Journal of the American Chemical Society. 124:14571-14579
Structural and functional roles of the hydrogen bonding network that surrounds the heme-thiolate coordination of P450(cam) from Pseudomonas putida were investigated. A hydrogen bond between the side chain amide of Gln360 and the carbonyl oxygen of th