SwePub
Sök i LIBRIS databas

  Utökad sökning

onr:"swepub:oai:DiVA.org:su-181761"
 

Sökning: onr:"swepub:oai:DiVA.org:su-181761" > Key Structural Moti...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004549naa a2200505 4500
001oai:DiVA.org:su-181761
003SwePub
008200527s2020 | |||||||||||000 ||eng|
009oai:DiVA.org:uu-411216
009oai:prod.swepub.kib.ki.se:143444844
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1817612 URI
0247 a https://doi.org/10.1021/jacs.0c003332 DOI
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4112162 URI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:1434448442 URI
040 a (SwePub)sud (SwePub)uud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Kisgeropoulos, Effie C.u Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA.4 aut
2451 0a Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein
264 c 2020-02-17
264 1b American Chemical Society (ACS),c 2020
338 a print2 rdacarrier
520 a Heterobimetallic Mn/Fe proteins represent a new cofactor paradigm in bioinorganic chemistry and pose countless outstanding questions. The assembly of the active site defies common chemical convention by contradicting the Irving-Williams series, while the scope of reactivity remains unexplored. In this work, the assembly and C-H bond activation process in the Mn/Fe R2-like ligand-binding oxidase (R2lox) protein is investigated using a suite of biophysical techniques, including time-resolved optical spectroscopy, global kinetic modeling, X-ray crystallography, electron paramagnetic resonance spectroscopy, protein electrochemistry, and mass spectrometry. Selective metal binding is found to be under thermodynamic control, with the binding sites within the apoprotein exhibiting greater Mn-II affinity than Fe-II affinity. The comprehensive analysis of structure and reactivity of wild-type R2lox and targeted primary and secondary sphere mutants indicate that the efficiency of C-H bond activation directly correlates with the Mn/Fe cofactor reduction potentials and is inversely related to divalent metal binding affinity. These findings suggest the R2lox active site is precisely tuned for achieving both selective heterobimetallic binding and high levels of reactivity and offer a mechanism to examine the means by which proteins achieve appropriate metal incorporation.
650 7a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe
650 7a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng
650 7a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng
650 7a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng
7001 a Griese, Julia J.u Uppsala universitet,Stockholms universitet,Institutionen för biokemi och biofysik,Uppsala University, Sweden,Strukturbiologi,Stockholm Univ, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden4 aut0 (Swepub:uu)julgr393
7001 a Smith, Zachary R.u Ohio State Univ, Dept Chem & Biochem, Columbus, OH 43210 USA.4 aut
7001 a Branca, Rui M. M.u Karolinska Institutet4 aut
7001 a Schneider, Camille R.u Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA.4 aut
7001 a Högbom, Martinu Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden.4 aut0 (Swepub:su)hogbom
7001 a Shafaat, Hannah S.u Ohio State Univ, Dept Chem & Biochem, Columbus, OH 43210 USA.;Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA.4 aut
7102 a Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA.b Institutionen för biokemi och biofysik4 org
7730 t Journal of the American Chemical Societyd : American Chemical Society (ACS)g 142:11, s. 5338-5354q 142:11<5338-5354x 0002-7863x 1520-5126
8564 u https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7390604
8564 u https://uu.diva-portal.org/smash/get/diva2:1433804/FULLTEXT02.pdfx primaryx Raw objecty fulltext:postprint
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-181761
8564 8u https://doi.org/10.1021/jacs.0c00333
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-411216
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:143444844

Hitta via bibliotek

Till lärosätets databas

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy