Sökning: WFRF:(Olesen Kenneth 1966) > (2005) > High resolution X-r...
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000 | 03780naa a2200529 4500 | |
001 | oai:gup.ub.gu.se/25762 | |
003 | SwePub | |
008 | 240528s2005 | |||||||||||000 ||eng| | |
009 | oai:research.chalmers.se:e9022e31-b8cf-4e8b-a19b-efcf1016f69e | |
024 | 7 | a https://gup.ub.gu.se/publication/257622 URI |
024 | 7 | a https://doi.org/10.1107/S09074449050174882 DOI |
024 | 7 | a https://research.chalmers.se/publication/257622 URI |
040 | a (SwePub)gud (SwePub)cth | |
041 | a eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Jacobson, Frida,d 1975u Chalmers tekniska högskola,Chalmers University of Technology4 aut |
245 | 1 0 | a High resolution X-ray structures of the oxidised and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 |
264 | 1 | c 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 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
650 | 7 | a 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 | |
700 | 1 | a Guo, Ku AstraZeneca AB4 aut |
700 | 1 | a 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 |
700 | 1 | a Ökvist, Mats,d 1970u Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg4 aut |
700 | 1 | a Neutze, Richard,d 1969u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)xneuri |
700 | 1 | a Sjölin, Lennart,d 1949u Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg4 aut0 (Swepub:gu)xsjoll |
710 | 2 | a Chalmers tekniska högskolab AstraZeneca AB4 org |
773 | 0 | t Acta Crystallography Dg 61, s. 1190-1198q 61<1190-1198x 0907-4449x 1399-0047 |
856 | 4 | u http://dx.doi.org/10.1107/S0907444905017488y FULLTEXT |
856 | 4 8 | u https://gup.ub.gu.se/publication/25762 |
856 | 4 8 | u https://doi.org/10.1107/S0907444905017488 |
856 | 4 8 | u https://research.chalmers.se/publication/25762 |
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