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Recognizing and predicting general t...
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Lucchese, Baldo.
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Recognizing and predicting general trends in the reactivity and chemistry of a series of related copper complexes.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Recognizing and predicting general trends in the reactivity and chemistry of a series of related copper complexes./
作者:
Lucchese, Baldo.
面頁冊數:
228 p.
附註:
Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0707.
Contained By:
Dissertation Abstracts International64-02B.
標題:
Chemistry, Inorganic. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3080720
Recognizing and predicting general trends in the reactivity and chemistry of a series of related copper complexes.
Lucchese, Baldo.
Recognizing and predicting general trends in the reactivity and chemistry of a series of related copper complexes.
- 228 p.
Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0707.
Thesis (Ph.D.)--The Johns Hopkins University, 2003.
Copper metallo-proteins play fundamental roles in the biology of organisms in every level of the evolutionary ladder. As part of the research effort aimed at uncovering and understanding the general rules and factors governing the reactivity displayed by copper in these proteins, a biomimetic approach has been utilized. A number of interrelated mono-, bi- and trinuclear copper complexes have been synthesized and studied, which might be relevant to the mono-, di- and tri-copper sites found in naturally occurring copper proteins.Subjects--Topical Terms:
517253
Chemistry, Inorganic.
Recognizing and predicting general trends in the reactivity and chemistry of a series of related copper complexes.
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Copper metallo-proteins play fundamental roles in the biology of organisms in every level of the evolutionary ladder. As part of the research effort aimed at uncovering and understanding the general rules and factors governing the reactivity displayed by copper in these proteins, a biomimetic approach has been utilized. A number of interrelated mono-, bi- and trinuclear copper complexes have been synthesized and studied, which might be relevant to the mono-, di- and tri-copper sites found in naturally occurring copper proteins.
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Chapter 1 introduces the structure and function as well as mechanistic insights of a number of multinuclear copper proteins whose main role is to bind dioxygen, in most cases to activate it in order to oxidize or oxygenate organic as well as inorganic substrates. An account of the role that biomimetic chemistry has had historically in the study of these proteins is given along with proposed research.
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Chapter 2 includes the synthesis and characterization of a series of mono-, di- and trinuclear CuII complexes by way of the environmentally relevant reaction of reductive dechlorination of chloroform performed by the corresponding cuprous complexes. Mechanistic insights into this reactivity are also pursued.
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Chapter 3 explores the reactivity towards dioxygen of a series of Cu I complexes at low temperature. Reactivity studies (comparative as well as non-comparative) towards external substrates of a low-temperature-stable and a low-temperature-unstable end-on peroxo dicopper(II) adduct, are also discussed.
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Chapter 4 introduces an approach to explain and predict geometric distortions in the coordination environments of 5-coordinate CuII complexes as a function of the structure of the chelating tetradentate ligand. These distortions seem to have a direct effect on the kinetic stability and reactivity of the dioxygen adducts formed by these copper complexes.
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Chapter 5 reinvestigates the low temperature reactivity towards dioxygen of the copper(I) complex of a monucleating tripodal tetradentate ligand. Reinvestigation is prompted by new literature data on a related system. Proof of the formation of a mixture of two 2:1 Cu/O2 adducts, an end-on peroxo dicopper(II) and a bis(m-oxo)dicopper(III) (as opposed to the originally reported formation of a 1:1 CuII-superoxo adduct), is provided.
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