| Year |
Citation |
Score |
| 2021 |
Copeland RA, Davis KM, Shoda TKC, Blaesi EJ, Boal AK, Krebs C, Bollinger JM. An Iron(IV)-Oxo Intermediate Initiating l-Arginine Oxidation but Not Ethylene Production by the 2-Oxoglutarate-Dependent Oxygenase, Ethylene-Forming Enzyme. Journal of the American Chemical Society. PMID 33522811 DOI: 10.1021/jacs.0c10923 |
0.481 |
|
| 2019 |
Cutsail GE, Blaesi EJ, Pollock CJ, Bollinger JM, Krebs C, DeBeer S. High-resolution iron X-ray absorption spectroscopic and computational studies of non-heme diiron peroxo intermediates. Journal of Inorganic Biochemistry. 203: 110877. PMID 31710865 DOI: 10.1016/J.Jinorgbio.2019.110877 |
0.508 |
|
| 2019 |
Zhang B, Rajakovich LJ, Van Cura D, Blaesi EJ, Mitchell AJ, Tysoe CR, Zhu X, Streit BR, Rui Z, Zhang W, Boal AK, Krebs C, Bollinger JM. Substrate-triggered Formation of a Peroxo-Fe(III/III) Intermediate during Fatty Acid Decarboxylation by UndA. Journal of the American Chemical Society. PMID 31487162 DOI: 10.1021/Jacs.9B06093 |
0.617 |
|
| 2019 |
McQuarters AB, Blaesi EJ, Kampf JW, Alp EE, Zhao J, Hu M, Krebs C, Lehnert N. Synthetic Model Complex of the Key Intermediate in Cytochrome P450 Nitric Oxide Reductase. Inorganic Chemistry. PMID 30623648 DOI: 10.1021/Acs.Inorgchem.8B02947 |
0.606 |
|
| 2018 |
Blaesi EJ, Palowitch GM, Hu K, Kim AJ, Rose HR, Alapati R, Lougee MG, Kim HJ, Taguchi AT, Tan KO, Laremore TN, Griffin RG, Krebs C, Matthews ML, Silakov A, et al. Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical. Proceedings of the National Academy of Sciences of the United States of America. PMID 30224458 DOI: 10.1073/Pnas.1811993115 |
0.451 |
|
| 2018 |
Grell TAJ, Kincannon WM, Bruender NA, Blaesi EJ, Krebs C, Bandarian V, Drennan CL. Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. The Journal of Biological Chemistry. PMID 30217813 DOI: 10.1074/Jbc.Ra118.005369 |
0.462 |
|
| 2018 |
Martinie RJ, Blaesi EJ, Bollinger JM, Krebs C, Finkelstein KD, Pollock C. Two-Color Valence-to-Core X-ray Emission Spectroscopy Tracks Cofactor Protonation State in a Class I Ribonucleotide Reductase. Angewandte Chemie (International Ed. in English). PMID 30075052 DOI: 10.1002/Anie.201807366 |
0.427 |
|
| 2018 |
Wang B, Blaszczyk AJ, Knox H, Zhou S, Blaesi EJ, Krebs C, Wang R, Booker SJ. Stereochemical and Mechanistic Investigation of the Reaction Catalyzed by Fom3 from Streptomyces fradiae, a Cobalamin-Dependent Radical S-Adenosylmethionine Methylase. Biochemistry. PMID 30036047 DOI: 10.1021/Acs.Biochem.8B00693 |
0.401 |
|
| 2018 |
Rose H, Ghosh M, Maggiolo A, Pollock CJ, Blaesi EJ, Hajj V, Wei Y, Rajakovich LJ, Chang WC, Han Y, Hajj M, Krebs C, Silakov A, Pandelia ME, Bollinger JM, et al. Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by its Dimanganese Cofactor. Biochemistry. PMID 29609464 DOI: 10.1021/Acs.Biochem.8B00247 |
0.373 |
|
| 2017 |
Miller EK, Trivelas NE, Maugeri PT, Blaesi EJ, Shafaat HS. Time-Resolved Investigations of Heterobimetallic Cofactor Assembly in R2lox Reveal Distinct Mn/Fe Intermediates. Biochemistry. PMID 28574263 DOI: 10.1021/Acs.Biochem.7B00403 |
0.598 |
|
| 2017 |
Martinie RJ, Blaesi EJ, Krebs C, Bollinger JM, Silakov A, Pollock CJ. Evidence for a Di-μ-oxo Diamond Core in the Mn(IV)/Fe(IV) Activation Intermediate of Ribonucleotide Reductase from Chlamydia trachomatis. Journal of the American Chemical Society. 139: 1950-1957. PMID 28075562 DOI: 10.1021/Jacs.6B11563 |
0.666 |
|
| 2015 |
Blaesi EJ, Fox BG, Brunold TC. Spectroscopic and Computational Investigation of the H155A Variant of Cysteine Dioxygenase: Geometric and Electronic Consequences of a Third-Sphere Amino Acid Substitution. Biochemistry. 54: 2874-84. PMID 25897562 DOI: 10.1021/Acs.Biochem.5B00171 |
0.672 |
|
| 2014 |
Blaesi EJ, Fox BG, Brunold TC. Spectroscopic and computational investigation of iron(III) cysteine dioxygenase: implications for the nature of the putative superoxo-Fe(III) intermediate. Biochemistry. 53: 5759-70. PMID 25093959 DOI: 10.1021/Bi500767X |
0.672 |
|
| 2013 |
Li W, Blaesi EJ, Pecore MD, Crowell JK, Pierce BS. Second-sphere interactions between the C93-Y157 cross-link and the substrate-bound Fe site influence the Oâ‚‚ coupling efficiency in mouse cysteine dioxygenase. Biochemistry. 52: 9104-19. PMID 24279989 DOI: 10.1021/Bi4010232 |
0.574 |
|
| 2013 |
Blaesi EJ, Gardner JD, Fox BG, Brunold TC. Spectroscopic and computational characterization of the NO adduct of substrate-bound Fe(II) cysteine dioxygenase: insights into the mechanism of O2 activation. Biochemistry. 52: 6040-51. PMID 23906193 DOI: 10.1021/Bi400825C |
0.596 |
|
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