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Sökning: WFRF:(Olesen Kenneth 1966) > (2005) > High resolution X-r...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003780naa a2200529 4500
001oai:gup.ub.gu.se/25762
003SwePub
008240528s2005 | |||||||||||000 ||eng|
009oai:research.chalmers.se:e9022e31-b8cf-4e8b-a19b-efcf1016f69e
024a https://gup.ub.gu.se/publication/257622 URI
024a https://doi.org/10.1107/S09074449050174882 DOI
024a https://research.chalmers.se/publication/257622 URI
040 a (SwePub)gud (SwePub)cth
041 a eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Jacobson, Frida,d 1975u Chalmers tekniska högskola,Chalmers University of Technology4 aut
2451 0a High resolution X-ray structures of the oxidised and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3
264 1c 2005
520 a Nitrite reductase is an enzyme operating in the denitrification pathway which catalyses the conversion of nitrite (NO2(-)) to gaseous nitric oxide (NO). Here, crystal structures of the oxidized and reduced forms of the copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3 are presented at 1.74 and 1.85 A resolution, respectively. Whereas the structure of the enzyme is very similar to those of other copper-containing nitrite reductases, folding as a trimer and containing two copper sites per monomer, the structures reported here enable conformational differences between the oxidized and reduced forms of the enzyme to be identified. In the type 1 copper site, a rotational perturbation of the side chain of the copper ligand Met182 occurs upon reduction. At the type 2 copper site, a dual conformation of the catalytic residue His287 is observed in the oxidized structure but is lacking in the reduced structure, such that the interactions of the oxidized type 2 copper ion can be regarded as adopting octahedral geometry. These findings shed light on the structural mechanism of the reduction of a copper-bound nitrite to nitric oxide and water.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653 a Copper
653 a chemistry
653 a Crystallography
653 a X-Ray
653 a Hydrogen-Ion Concentration
653 a Nitrite Reductases
653 a chemistry
653 a metabolism
653 a Oxidation-Reduction
653 a Protein Conformation
653 a Rhodobacter sphaeroides
653 a enzymology
653 a Rhodobacter sphaeroides
700a Guo, Ku AstraZeneca AB4 aut
700a Olesen, Kenneth,d 1966u Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry,University of Gothenburg4 aut0 (Swepub:gu)xoleke
700a Ökvist, Mats,d 1970u Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg4 aut
700a Neutze, Richard,d 1969u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)xneuri
700a Sjölin, Lennart,d 1949u Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg4 aut0 (Swepub:gu)xsjoll
710a Chalmers tekniska högskolab AstraZeneca AB4 org
773t Acta Crystallography Dg 61, s. 1190-1198q 61<1190-1198x 0907-4449x 1399-0047
856u http://dx.doi.org/10.1107/S0907444905017488y FULLTEXT
8564 8u https://gup.ub.gu.se/publication/25762
8564 8u https://doi.org/10.1107/S0907444905017488
8564 8u https://research.chalmers.se/publication/25762

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