Itoh Group Literature Review

Koji Oohora,*,†,‡,§ Hiroyuki Meichin,† Yushi Kihira,† Hiroshi Sugimoto,∥ Yoshitsugu Shiro,∥,⊥ and Takashi Hayashi DOI: 10.1021/jacs.7b11288 http://pubs.acs.org/doi/10.1021/jacs.7b11288 Jacsから、林研の大洞先生の論文です。 ミオグロビンにポルフィセンのマンガン錯体を導入し、酸化活性種の同定および酸化反応を行っています。 過酸を酸化剤としてマンガンオキソ錯体が生成し、BDE95程度まで酸化できるようです。 中間体の寿命が伸びたことが今回の系では効いているとのことです。

Summer A. Baker Dockrey 1,2 , April L. Lukowski 2,3 , Marc R. Becker 1 and Alison R. H. Narayan 1,2,3 * 1 Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA. 2 Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109, USA. 3 Program in Chemical Biology, University of Michigan, Ann Arbor, Michigan 48109, USA. doi :10.1038/nchem.2879      https://www.nature.com/articles/nchem.2879 酵素触媒によるフェノールの酸化反応についてです。 選択性、基質適合性、合成スケールが合成化学的にも有用なほど優れているようです。

Angew.andte Reviews Angew. Chem. Int. Ed. 2015, 54, 3351 – 3367 Hans Renata, Z. Jane Wang, and Frances H. Arnold Division of Chemistry and Chemical Engineering California Institute of Technology 1200 E. California Blvd. MC 210-41, Pasadena, CA 91125 (USA) http://onlinelibrary.wiley.com/doi/10.1002/anie.201409470/pdf Abstruction High selectivity and exquisite control over the outcome of reactions entice chemists to use biocatalysts in organic synthesis. However, many useful reactions are not accessible because they are not in nature s known repertoire. In this Review, we outline an evolutionary approach to engineering enzymes to catalyze reactions not found in nature. We begin with examples of how nature has discovered new catalytic functions and how such evolutionary progression has been recapitulated in the laboratory starting from extant enzymes. We then examine non-native enzyme activities that have been exploited for chemical synthesis, with an emphasis on reac...

Rae Ana Snyder † , Justine Betzu ‡ , Susan E. Butch ‡ , Amanda J. Reig * ‡ , William F. DeGrado * § , and Edward I. Solomon * † ∥ † Department of Chemistry, Stanford University , Stanford, California 94305, United States ‡ Department of Chemistry, Ursinus College , Collegeville, Pennsylvania 19426, United States § Department of Pharmaceutical Chemistry, University of California San Francisco , San Francisco, California 94143, United States ∥ Stanford Synchrotron Radiation Laboratory, Stanford University, SLAC , Menlo Park, California 94025, United States Biochemistry , Article ASAP DOI: 10.1021/acs.biochem.5b00324 Publication Date (Web): July 8, 2015 Copyright © 2015 American Chemical Society *E-mail: areig@ursinus.edu . Phone: (610) 409-3383 ., *E-mail: Bill.DeGrado@ucsf.edu . Phone: (415) 476-9679 ., *E-mail: edward.solomon@stanford.edu . Phone: (650) 723-9104 . Abstract DFsc (single-chain due ferri ) proteins allow for modeling binuclear non...

Sarah A. Cook , Ethan A. Hill , and A. S. Borovik *   Department of Chemistry, University of California—Irvine , 1102 Natural Sciences II, Irvine, California 92697, United States Biochemistry , Article ASAP DOI: 10.1021/acs.biochem.5b00249 Publication Date (Web): June 16, 2015 Copyright © 2015 American Chemical Society *E-mail: aborovik@uci.edu . Phone: (949) 824-1510 . Abstract Metalloproteins contain actives sites with intricate structures that perform specific functions with high selectivity and efficiency. The complexity of these systems complicates the study of their function and the understanding of the properties that give rise to their reactivity. One approach that has contributed to the current level of understanding of their biological function is the study of synthetic constructs that mimic one or more aspects of the native metalloproteins. These systems allow individual contributions to the structure and function to be analyzed and als...

Biochemistry: Latest Articles (ACS ... by Yan Li, Miroslav Hodak and J. Bernholc  /  6h  //  keep unread  //  hide  //  preview   Biochemistry DOI: 10.1021/bi500776   Abstract Copper-containing nitrite reductases (CuNiRs) catalyze the reduction of nitrite to nitric oxide, a key step in the denitrification process that maintains balance between organic and inorganic nitrogen. Despite their importance, their functioning is not well understood. In this work, we carry out first-principles calculations and show that the available structural data are consistent only with a single mechanism. For this mechanism, we determine the activation energies, transition states, and minimum energy pathways of CuNiR. The calculations lead to an updated enzymatic mechanism and resolve several controversial issues. In particular, our work identifies the origins of the two protons necessary for the enzymatic function ...