Binuclear Copper A : Part 6. Copper ; Binuclear Copper : CuA Copper

dc.contributor.authorKroneck, Peter M. H.
dc.date.accessioned2017-06-13T09:26:30Z
dc.date.available2017-06-13T09:26:30Z
dc.date.issued2006eng
dc.description.abstractThe purple CuA is a Cys-bridged, mixed-valence electron transfer center [Cu(1.5+)…Cu(1.5+)], found in cytochrome c oxidase and in nitrous oxide reductase. More recently, the NO reductase from Bacillus azotoformans was identified as the third CuA-containing enzyme. There also exist engineered CuA sites which have been introduced by loop-directed mutagenesis into blue type 1 copper proteins, such as azurin or amicyanin. Electron transfer mediated by CuA is very efficient. The reasons for utilizing a binuclear electron transfer center in cytochrome c oxidase and nitrous oxide reductase, instead of mononuclear type 1 Cu, are suggested to be its unidirectional electron transfer through the site or the lower energy of reorganization. Interest in CuA is directly related to its unique spectroscopic properties. Studies by paramagnetic resonance, magnetic circular dichroism, resonance Raman, and X-ray absorption spectroscopy have provided a clear picture of the electronic properties of the CuA site and the interaction of the metal atoms with the neighboring amino acids.eng
dc.description.versionpublishedeng
dc.identifier.doi10.1002/0470028637.met197eng
dc.identifier.urihttps://kops.uni-konstanz.de/handle/123456789/39247
dc.language.isoengeng
dc.subjectcopper A;mixed-valence;Cu2S2 rhomb;electron transfer;binuclear centereng
dc.subject.ddc570eng
dc.titleBinuclear Copper A : Part 6. Copper ; Binuclear Copper : CuA Coppereng
dc.typeINCOLLECTIONeng
dspace.entity.typePublication
kops.citation.bibtex
@incollection{Kroneck2006Binuc-39247,
  year={2006},
  doi={10.1002/0470028637.met197},
  title={Binuclear Copper A : Part 6. Copper ; Binuclear Copper : CuA Copper},
  isbn={978-0-470-86981-9},
  publisher={John Wiley & Sons, Ltd},
  address={Chichester},
  booktitle={Handbook of Metalloproteins},
  editor={Messerschmidt, Albrecht and Huber, Robert and Poulas, Thomas and Wieghardt, Karl and Cygler, Mirek and Bode, Wolfram},
  author={Kroneck, Peter M. H.}
}
kops.citation.iso690KRONECK, Peter M. H., 2006. Binuclear Copper A : Part 6. Copper ; Binuclear Copper : CuA Copper. In: MESSERSCHMIDT, Albrecht, ed., Robert HUBER, ed., Thomas POULAS, ed., Karl WIEGHARDT, ed., Mirek CYGLER, ed., Wolfram BODE, ed.. Handbook of Metalloproteins. Chichester: John Wiley & Sons, Ltd, 2006. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met197deu
kops.citation.iso690KRONECK, Peter M. H., 2006. Binuclear Copper A : Part 6. Copper ; Binuclear Copper : CuA Copper. In: MESSERSCHMIDT, Albrecht, ed., Robert HUBER, ed., Thomas POULAS, ed., Karl WIEGHARDT, ed., Mirek CYGLER, ed., Wolfram BODE, ed.. Handbook of Metalloproteins. Chichester: John Wiley & Sons, Ltd, 2006. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met197eng
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    <dcterms:abstract xml:lang="eng">The purple CuA is a Cys-bridged, mixed-valence electron transfer center [Cu(1.5+)…Cu(1.5+)], found in cytochrome c oxidase and in nitrous oxide reductase. More recently, the NO reductase from Bacillus azotoformans was identified as the third CuA-containing enzyme. There also exist engineered CuA sites which have been introduced by loop-directed mutagenesis into blue type 1 copper proteins, such as azurin or amicyanin. Electron transfer mediated by CuA is very efficient. The reasons for utilizing a binuclear electron transfer center in cytochrome c oxidase and nitrous oxide reductase, instead of mononuclear type 1 Cu, are suggested to be its unidirectional electron transfer through the site or the lower energy of reorganization. Interest in CuA is directly related to its unique spectroscopic properties. Studies by paramagnetic resonance, magnetic circular dichroism, resonance Raman, and X-ray absorption spectroscopy have provided a clear picture of the electronic properties of the CuA site and the interaction of the metal atoms with the neighboring amino acids.</dcterms:abstract>
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kops.sourcefieldMESSERSCHMIDT, Albrecht, ed., Robert HUBER, ed., Thomas POULAS, ed., Karl WIEGHARDT, ed., Mirek CYGLER, ed., Wolfram BODE, ed.. <i>Handbook of Metalloproteins</i>. Chichester: John Wiley & Sons, Ltd, 2006. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met197deu
kops.sourcefield.plainMESSERSCHMIDT, Albrecht, ed., Robert HUBER, ed., Thomas POULAS, ed., Karl WIEGHARDT, ed., Mirek CYGLER, ed., Wolfram BODE, ed.. Handbook of Metalloproteins. Chichester: John Wiley & Sons, Ltd, 2006. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met197deu
kops.sourcefield.plainMESSERSCHMIDT, Albrecht, ed., Robert HUBER, ed., Thomas POULAS, ed., Karl WIEGHARDT, ed., Mirek CYGLER, ed., Wolfram BODE, ed.. Handbook of Metalloproteins. Chichester: John Wiley & Sons, Ltd, 2006. ISBN 978-0-470-86981-9. Available under: doi: 10.1002/0470028637.met197eng
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source.contributor.editorMesserschmidt, Albrecht
source.contributor.editorHuber, Robert
source.contributor.editorPoulas, Thomas
source.contributor.editorWieghardt, Karl
source.contributor.editorCygler, Mirek
source.contributor.editorBode, Wolfram
source.identifier.isbn978-0-470-86981-9eng
source.publisherJohn Wiley & Sons, Ltdeng
source.publisher.locationChichestereng
source.titleHandbook of Metalloproteinseng

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