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Electronic structures of active sites in copper proteins : contributions to reactivity
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This article is published in Chemical Reviews.The article was published on 1992-06-01. It has received 838 citations till now. The article focuses on the topics: Reactivity (chemistry) & Copper protein.read more
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Multicopper Oxidases and Oxygenases
TL;DR: Copper sites have historically been divided into three classes based on their spectroscopic features, which reflect the geometric and electronic structure of the active site: type 1 or blue copper, type 2 (T2) or normal copper, and type 3 (T3) or coupled binuclear copper centers.
Journal ArticleDOI
Activation of c-h bonds by metal complexes
A. E. Shilov,Georgiy B. Shul'pin +1 more
TL;DR: In this article, it was shown that the same alkylhydridoplatinum(IV) complex is the intermediate in the reaction of ethane with platinum(II) σ-complexes.
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The Mononuclear Molybdenum Enzymes
TL;DR: It is now well-established that all molybdenum-containing enzymes other than nitrogenase fall into three large and mutually exclusive families, as exemplified by the enzymes xanthine oxidation, sulfite oxidase, and DMSO reductase; these enzymes represent the focus of the present account.
Journal ArticleDOI
Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes
Edward I. Solomon,Thomas C. Brunold,Mindy I. Davis,Jyllian N. Kemsley,Sang-Kyu Lee,Nicolai Lehnert,Frank Neese,Andrew J. Skulan,Yi-Shan Yang,Jing Zhou +9 more
TL;DR: A detailed molecular mechanism has been proposed for IPNS based on spectroscopic and crystallographic studies and the role of cosubstrate ascorbate is proposed to reduce the toxic peroxo byproduct to water.