Sökning: WFRF:(Griese M.) > Key Structural Moti...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 04549naa a2200505 4500 | |
001 | oai:DiVA.org:su-181761 | |
003 | SwePub | |
008 | 200527s2020 | |||||||||||000 ||eng| | |
009 | oai:DiVA.org:uu-411216 | |
009 | oai:prod.swepub.kib.ki.se:143444844 | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1817612 URI |
024 | 7 | a https://doi.org/10.1021/jacs.0c003332 DOI |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4112162 URI |
024 | 7 | 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 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Kisgeropoulos, Effie C.u Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA.4 aut |
245 | 1 0 | a Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein |
264 | c 2020-02-17 | |
264 | 1 | b 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 | 7 | a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng |
650 | 7 | a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng |
650 | 7 | a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng |
700 | 1 | 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 |
700 | 1 | a Smith, Zachary R.u Ohio State Univ, Dept Chem & Biochem, Columbus, OH 43210 USA.4 aut |
700 | 1 | a Branca, Rui M. M.u Karolinska Institutet4 aut |
700 | 1 | a Schneider, Camille R.u Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA.4 aut |
700 | 1 | a Högbom, Martinu Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden.4 aut0 (Swepub:su)hogbom |
700 | 1 | 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 |
710 | 2 | a Ohio State Univ, Ohio State Biochem Program, Columbus, OH 43210 USA.b Institutionen för biokemi och biofysik4 org |
773 | 0 | 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 |
856 | 4 | u https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7390604 |
856 | 4 | u https://uu.diva-portal.org/smash/get/diva2:1433804/FULLTEXT02.pdfx primaryx Raw objecty fulltext:postprint |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-181761 |
856 | 4 8 | u https://doi.org/10.1021/jacs.0c00333 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-411216 |
856 | 4 8 | u http://kipublications.ki.se/Default.aspx?queryparsed=id:143444844 |
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.
Kopiera och spara länken för att återkomma till aktuell vy