Matches in SemOpenAlex for { <https://semopenalex.org/work/W2080493328> ?p ?o ?g. }
- W2080493328 endingPage "4779" @default.
- W2080493328 startingPage "4760" @default.
- W2080493328 abstract "1.1. BackgroundThe use of copper in biological systems coincides with the advent of an oxygen atmosphere about 1.7 billion years ago. The presence of O2 both allowed the oxidation of insoluble Cu(I) to the more soluble and bioavailable Cu(II) and led to the requirement for a redox active metal with potentials in the 0-800 mV range. Not only did copper meet this need, but the oxidation of Fe(II) to the insoluble Fe(III) form rendered the use of iron more energetically expensive.1-5 As a result, copper plays a key role in many proteins that react with O2. Generally, O2-reactive centers are mononuclear (type 2), dinuclear (type 3), or trinuclear (type 2 and type 3). Well studied mononuclear copper enzymes include the monooxygenases dopamine-β-hydroxylase and peptidylglycine α-hydroxylating monooxygenase as well as oxidases that also contain organic cofactors, such as amine, galactose, and lysyl oxidases.6 Dinuclear copper proteins include the O2 carrier hemocyanin and enzymes like tyrosinase and catechol oxidase.7 Copper also plays a key role in numerous electron transfer proteins. Mononuclear type 1 (blue copper) centers are found in proteins such as plastocyanin and azurin.8 The multicopper oxidases like laccase, ascorbate oxidase, and ceruloplasmin contain both a catalytic trinuclear type 2/type 3 site and an electron transfer type 1 site.9,10 The classification of copper centers into types is derived from optical and electron paramagnetic resonance (EPR) spectroscopic properties, and there are some notable exceptions, including the cysteine-bridged dinuclear CuA electron transfer site in cytochrome c oxidase11 and nitrous oxide reductase, the tetranuclear catalytic CuZ center in nitrous oxide reductase,12 and the proposed catalytic copper center in particulate methane monooxygenase.13-15The same redox properties that render copper useful in all these metalloproteins can lead to oxidative damage in cells. Reaction of Cu(I) with hydrogen peroxide and re-reduction of Cu(II) by superoxide via Fenton and Haber-Weiss chemistry yields hydroxyl radicals that can damage proteins, lipids, and nucleic acids.16 Thus, intracellular copper concentrations must be controlled such that copper ions are provided to essential enzymes, but do not accumulate to deleterious levels. In humans, deficiencies in copper metabolism are linked to diseases such as Menkes syndrome, Wilson disease, prion diseases, and Alzheimer’s disease.17 Several classes of proteins, including membrane transporters,18-20 metallochaperones,21,22 and metalloregulatory proteins,23,24 are implicated in copper homeostasis. These proteins have two functions. First, they ensure that copper is provided to the correct proteins and cellular compartments for necessary activities. Second, these proteins detoxify excess copper. Just as copper-containing proteins and enzymes are found in all kingdoms of life, members of these groups of homeostatic proteins are also widespread,5 and have been structurally and biochemically characterized from eukaryotes and prokaryotes." @default.
- W2080493328 created "2016-06-24" @default.
- W2080493328 creator A5000721117 @default.
- W2080493328 creator A5039479636 @default.
- W2080493328 date "2009-07-15" @default.
- W2080493328 modified "2023-10-18" @default.
- W2080493328 title "Structural Biology of Copper Trafficking" @default.
- W2080493328 cites W1489286950 @default.
- W2080493328 cites W1496283406 @default.
- W2080493328 cites W1514437369 @default.
- W2080493328 cites W1519459752 @default.
- W2080493328 cites W1547418730 @default.
- W2080493328 cites W1562297091 @default.
- W2080493328 cites W1585758755 @default.
- W2080493328 cites W1697966803 @default.
- W2080493328 cites W1735246691 @default.
- W2080493328 cites W1768948929 @default.
- W2080493328 cites W1869259273 @default.
- W2080493328 cites W1879184430 @default.
- W2080493328 cites W1884328895 @default.
- W2080493328 cites W1885185292 @default.
- W2080493328 cites W1963874808 @default.
- W2080493328 cites W1964180300 @default.
- W2080493328 cites W1964292121 @default.
- W2080493328 cites W1964670708 @default.
- W2080493328 cites W1964862882 @default.
- W2080493328 cites W1965135816 @default.
- W2080493328 cites W1965202020 @default.
- W2080493328 cites W1965249399 @default.
- W2080493328 cites W1966112781 @default.
- W2080493328 cites W1966732500 @default.
- W2080493328 cites W1968740095 @default.
- W2080493328 cites W1971182909 @default.
- W2080493328 cites W1971326367 @default.
- W2080493328 cites W1972148783 @default.
- W2080493328 cites W1974104912 @default.
- W2080493328 cites W1974415050 @default.
- W2080493328 cites W1974939001 @default.
- W2080493328 cites W1975183148 @default.
- W2080493328 cites W1976329674 @default.
- W2080493328 cites W1977316589 @default.
- W2080493328 cites W1978472424 @default.
- W2080493328 cites W1979323699 @default.
- W2080493328 cites W1982243317 @default.
- W2080493328 cites W1984156328 @default.
- W2080493328 cites W1986080062 @default.
- W2080493328 cites W1987849522 @default.
- W2080493328 cites W1988056859 @default.
- W2080493328 cites W1988710062 @default.
- W2080493328 cites W1988821469 @default.
- W2080493328 cites W1989137361 @default.
- W2080493328 cites W1989418680 @default.
- W2080493328 cites W1990181521 @default.
- W2080493328 cites W1990708284 @default.
- W2080493328 cites W1990729534 @default.
- W2080493328 cites W1991296029 @default.
- W2080493328 cites W1991335778 @default.
- W2080493328 cites W1993830119 @default.
- W2080493328 cites W1994007675 @default.
- W2080493328 cites W1994421318 @default.
- W2080493328 cites W1995491627 @default.
- W2080493328 cites W1997143231 @default.
- W2080493328 cites W1998080828 @default.
- W2080493328 cites W1999838269 @default.
- W2080493328 cites W2002863296 @default.
- W2080493328 cites W2003359441 @default.
- W2080493328 cites W2005535197 @default.
- W2080493328 cites W2008054715 @default.
- W2080493328 cites W2010355719 @default.
- W2080493328 cites W2010990082 @default.
- W2080493328 cites W2011388752 @default.
- W2080493328 cites W2012200803 @default.
- W2080493328 cites W2012373360 @default.
- W2080493328 cites W2012846325 @default.
- W2080493328 cites W2015584929 @default.
- W2080493328 cites W2016434557 @default.
- W2080493328 cites W2017142519 @default.
- W2080493328 cites W2019076201 @default.
- W2080493328 cites W2019870906 @default.
- W2080493328 cites W2019958839 @default.
- W2080493328 cites W2020716533 @default.
- W2080493328 cites W2029936308 @default.
- W2080493328 cites W2033223398 @default.
- W2080493328 cites W2033938388 @default.
- W2080493328 cites W2034758552 @default.
- W2080493328 cites W2035293624 @default.
- W2080493328 cites W2036208778 @default.
- W2080493328 cites W2037109359 @default.
- W2080493328 cites W2040045256 @default.
- W2080493328 cites W2041055869 @default.
- W2080493328 cites W2042060970 @default.
- W2080493328 cites W2043104518 @default.
- W2080493328 cites W2043551256 @default.
- W2080493328 cites W2046089177 @default.
- W2080493328 cites W2046274277 @default.
- W2080493328 cites W2046771108 @default.
- W2080493328 cites W2047523779 @default.
- W2080493328 cites W2047973301 @default.