| Year |
Citation |
Score |
| 2023 |
Slater JW, Lin CY, Neugebauer ME, McBride MJ, Sil D, Nair MA, Katch BJ, Boal AK, Chang MCY, Silakov A, Krebs C, Bollinger JM. Synergistic Binding of the Halide and Cationic Prime Substrate of l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States. Biochemistry. PMID 37542461 DOI: 10.1021/acs.biochem.3c00248 |
0.657 |
|
| 2023 |
Slater JW, Neugebauer ME, McBride MJ, Sil D, Lin CY, Katch BJ, Boal AK, Chang MCY, Silakov A, Krebs C, Bollinger JM. Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States. Biorxiv : the Preprint Server For Biology. PMID 37205437 DOI: 10.1101/2023.05.02.539147 |
0.646 |
|
| 2023 |
Corrigan PS, Majer SH, Silakov A. Evidence of Atypical Structural Flexibility of the Active Site Surrounding of an [FeFe] Hydrogenase from . Journal of the American Chemical Society. 145: 11033-11044. PMID 37163727 DOI: 10.1021/jacs.2c13458 |
0.761 |
|
| 2023 |
Corrigan P, Silakov A. Anaerobic Infrared Spectroelectrochemical Methods for Studying Oxygen-Sensitive [FeFe] Hydrogenases. Methods in Molecular Biology (Clifton, N.J.). 2648: 43-62. PMID 37039984 DOI: 10.1007/978-1-0716-3080-8_4 |
0.675 |
|
| 2023 |
Brimberry M, Corrigan P, Silakov A, Lanzilotta WN. Evidence for Porphyrin-Mediated Electron Transfer in the Radical SAM Enzyme HutW. Biochemistry. PMID 36877586 DOI: 10.1021/acs.biochem.2c00474 |
0.704 |
|
| 2022 |
Lin CY, Muñoz AL, Laremore TN, Silakov A, Krebs C, Boal AK, Bollinger JM. Use of Noncanonical Tyrosine Analogues to Probe Control of Radical Intermediates during Endoperoxide Installation by Verruculogen Synthase (FtmOx1). Acs Catalysis. 12: 6968-6979. PMID 37744570 DOI: 10.1021/acscatal.2c01037 |
0.66 |
|
| 2021 |
Pang H, Walker LM, Silakov A, Zhang P, Yang W, Elliott SJ, Yokoyama K. Mechanism of Reduction of an Aminyl Radical Intermediate in the Radical SAM GTP 3',8-Cyclase MoaA. Journal of the American Chemical Society. PMID 34423974 DOI: 10.1021/jacs.1c06268 |
0.397 |
|
| 2020 |
Carl AG, Harris LD, Feng M, Nordstrøm LU, Gerfen GJ, Evans GB, Silakov A, Almo SC, Grove TL. Narrow-Spectrum Antibiotic Targeting of the Radical SAM Enzyme MqnE in Menaquinone Biosynthesis. Biochemistry. PMID 32627538 DOI: 10.1021/Acs.Biochem.0C00070 |
0.365 |
|
| 2020 |
Corrigan PS, Tirsch JL, Silakov A. Investigation of the Unusual Ability of the [FeFe] Hydrogenase from to Access an O-Protected State. Journal of the American Chemical Society. 142: 12409-12419. PMID 32580545 DOI: 10.1021/Jacs.0C04964 |
0.68 |
|
| 2020 |
Zhang B, Arcinas AJ, Radle MI, Silakov A, Booker SJ, Krebs C. The First Step in Catalysis of the Radical S-Adenosylmethionine Methylthiotransferase MiaB Yields an Intermediate with a [3Fe-4S]0-like Auxiliary Cluster. Journal of the American Chemical Society. PMID 31899624 DOI: 10.1021/Jacs.9B11093 |
0.423 |
|
| 2019 |
Esakova OA, Silakov A, Grove TL, Warui DM, Yennawar NH, Booker SJ. An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase. Journal of the American Chemical Society. PMID 31390192 DOI: 10.1021/Jacs.9B02513 |
0.444 |
|
| 2019 |
Gumkowski JD, Martinie RJ, Corrigan P, Pan J, Bauerle MR, Almarei M, Booker SJ, Silakov A, Krebs C, Boal AK. Analysis of RNA methylation by phylogenetically diverse Cfr radical SAM enzymes reveals an iron-binding accessory domain in a clostridial enzyme. Biochemistry. PMID 31246421 DOI: 10.1021/Acs.Biochem.9B00197 |
0.743 |
|
| 2018 |
Arcinas AJ, Maiocco SJ, Elliott SJ, Silakov A, Booker SJ. Ferredoxins as Interchangeable Redox Components in Support of MiaB, a Radical S-Adenosylmethionine Methylthiotransferase. Protein Science : a Publication of the Protein Society. PMID 30394621 DOI: 10.1002/Pro.3548 |
0.47 |
|
| 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 |
0.658 |
|
| 2018 |
Dunham NP, Chang WC, Mitchell AJ, Martinie RJ, Zhang B, Bergman JA, Rajakovich LJ, Wang B, Silakov A, Krebs C, Boal AK, Bollinger JM. Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of α-Heteroatom Assistance. Journal of the American Chemical Society. PMID 29708749 DOI: 10.1021/Jacs.8B01933 |
0.709 |
|
| 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 |
0.66 |
|
| 2017 |
Martinie RJ, Pollock CJ, Matthews ML, Bollinger JM, Krebs C, Silakov A. Vanadyl as a Stable Structural Mimic of Reactive Ferryl Intermediates in Mononuclear Nonheme-Iron Enzymes. Inorganic Chemistry. 56: 13382-13389. PMID 28960972 DOI: 10.1021/Acs.Inorgchem.7B02113 |
0.57 |
|
| 2017 |
Mitchell AJ, Dunham NP, Martinie RJ, Bergman JA, Pollock CJ, Hu K, Allen BD, Chang WC, Silakov A, Bollinger JM, Krebs C, Boal AK. Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase. Journal of the American Chemical Society. 139: 13830-13836. PMID 28823155 DOI: 10.1021/Jacs.7B07374 |
0.709 |
|
| 2017 |
Blaszczyk AJ, Wang B, Silakov A, Ho JV, Booker SJ. Efficient Methylation of C2 in L-Tryptophan by the Cobalamin-dependent Radical S-Adenosylmethionine Methylase TsrM Requires an Unmodified N1 Amine. The Journal of Biological Chemistry. PMID 28747433 DOI: 10.1074/Jbc.M117.778548 |
0.423 |
|
| 2017 |
Pistner AJ, Moon HW, Silakov A, Yennawar HP, Radosevich AT. Stable Open-Shell Phosphorane Based on a Redox-Active Amidodiphenoxide Scaffold. Inorganic Chemistry. PMID 28661124 DOI: 10.1021/Acs.Inorgchem.7B00657 |
0.392 |
|
| 2017 |
Onderko EL, Silakov A, Yosca TH, Green MT. Characterization of a selenocysteine-ligated P450 compound I reveals direct link between electron donation and reactivity. Nature Chemistry. 9: 623-628. PMID 28644466 DOI: 10.1038/Nchem.2781 |
0.774 |
|
| 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 |
0.523 |
|
| 2017 |
Yennawar N, Esakova O, Grove T, Silakov A, Saunders A, McLaughlin M, Booker S. A structural study of quinolinate synthase, a key enzyme in bacterial NAD+ biosynthesis Acta Crystallographica Section a Foundations and Advances. 73: a150-a150. DOI: 10.1107/S0108767317098518 |
0.318 |
|
| 2016 |
Esakova OA, Silakov A, Grove TL, Saunders AH, McLaughlin MI, Yennawar NH, Booker SJ. Structure of Quinolinate Synthase from Pyrococcus horikoshii in the Presence of Its Product, Quinolinic Acid. Journal of the American Chemical Society. PMID 27224840 DOI: 10.1021/Jacs.6B02708 |
0.416 |
|
| 2016 |
Speelman AL, Zhang B, Silakov A, Skodje KM, Alp EE, Zhao J, Hu MY, Kim E, Krebs C, Lehnert N. Unusual Synthetic Pathway for an {Fe(NO)2}(9) Dinitrosyl Iron Complex (DNIC) and Insight into DNIC Electronic Structure via Nuclear Resonance Vibrational Spectroscopy. Inorganic Chemistry. PMID 27203448 DOI: 10.1021/Acs.Inorgchem.6B00510 |
0.498 |
|
| 2016 |
Blaszczyk AJ, Silakov A, Zhang B, Maiocco SJ, Lanz ND, Kelly WL, Elliott SJ, Krebs C, Booker SJ. Spectroscopic and Electrochemical Characterization of the Iron-Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase. Journal of the American Chemical Society. PMID 26841310 DOI: 10.1021/Jacs.5B12592 |
0.535 |
|
| 2015 |
Lanz ND, Rectenwald JM, Wang B, Kakar ES, Laremore TN, Booker SJ, Silakov A. Characterization of a Radical Intermediate in Lipoyl Cofactor Biosynthesis. Journal of the American Chemical Society. PMID 26390103 DOI: 10.1021/Jacs.5B04387 |
0.511 |
|
| 2015 |
Krest CM, Silakov A, Rittle J, Yosca TH, Onderko EL, Calixto JC, Green MT. Significantly shorter Fe-S bond in cytochrome P450-I is consistent with greater reactivity relative to chloroperoxidase. Nature Chemistry. 7: 696-702. PMID 26291940 DOI: 10.1038/Nchem.2306 |
0.731 |
|
| 2015 |
Livada J, Martinie RJ, Dassama LM, Krebs C, Bollinger JM, Silakov A. Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase from Chlamydia trachomatis. The Journal of Physical Chemistry. B. 119: 13777-84. PMID 26087051 DOI: 10.1021/Acs.Jpcb.5B04067 |
0.412 |
|
| 2015 |
Kim J, Silakov A, Yennawar HP, Lear BJ. Structural, Electronic, and Magnetic Characterization of a Dinuclear Zinc Complex Containing TCNQ(-) and a μ-[TCNQ-TCNQ](2-) Ligand. Inorganic Chemistry. 54: 6072-4. PMID 26085029 DOI: 10.1021/Acs.Inorgchem.5B00808 |
0.312 |
|
| 2015 |
Martinie RJ, Livada J, Chang WC, Green MT, Krebs C, Bollinger JM, Silakov A. Experimental Correlation of Substrate Position with Reaction Outcome in the Aliphatic Halogenase, SyrB2. Journal of the American Chemical Society. 137: 6912-9. PMID 25965587 DOI: 10.1021/Jacs.5B03370 |
0.592 |
|
| 2014 |
Silakov A, Grove TL, Radle MI, Bauerle MR, Green MT, Rosenzweig AC, Boal AK, Booker SJ. Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. Journal of the American Chemical Society. 136: 8221-8. PMID 24806349 DOI: 10.1021/Ja410560P |
0.683 |
|
| 2013 |
Yosca TH, Rittle J, Krest CM, Onderko EL, Silakov A, Calixto JC, Behan RK, Green MT. Iron(IV)hydroxide pK(a) and the role of thiolate ligation in C-H bond activation by cytochrome P450. Science (New York, N.Y.). 342: 825-9. PMID 24233717 DOI: 10.1126/Science.1244373 |
0.699 |
|
| 2013 |
Dassama LM, Silakov A, Krest CM, Calixto JC, Krebs C, Bollinger JM, Green MT. A 2.8 Å Fe-Fe separation in the Fe2(III/IV) intermediate, X, from Escherichia coli ribonucleotide reductase. Journal of the American Chemical Society. 135: 16758-61. PMID 24094084 DOI: 10.1021/Ja407438P |
0.785 |
|
| 2013 |
Wörsdörfer B, Conner DA, Yokoyama K, Livada J, Seyedsayamdost M, Jiang W, Silakov A, Stubbe J, Bollinger JM, Krebs C. Function of the diiron cluster of Escherichia coli class Ia ribonucleotide reductase in proton-coupled electron transfer. Journal of the American Chemical Society. 135: 8585-93. PMID 23676140 DOI: 10.1021/Ja401342S |
0.452 |
|
| 2013 |
Grove TL, Livada J, Schwalm EL, Green MT, Booker SJ, Silakov A. A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr. Nature Chemical Biology. 9: 422-7. PMID 23644479 DOI: 10.1038/Nchembio.1251 |
0.502 |
|
| 2012 |
Adamska A, Silakov A, Lambertz C, Rüdiger O, Happe T, Reijerse E, Lubitz W. Identification and characterization of the "super-reduced" state of the H-cluster in [FeFe] hydrogenase: a new building block for the catalytic cycle? Angewandte Chemie (International Ed. in English). 51: 11458-62. PMID 23109267 DOI: 10.1002/Anie.201204800 |
0.334 |
|
| 2012 |
Silakov A, Olsen MT, Sproules S, Reijerse EJ, Rauchfuss TB, Lubitz W. EPR/ENDOR, Mössbauer, and quantum-chemical investigations of diiron complexes mimicking the active oxidized state of [FeFe]hydrogenase. Inorganic Chemistry. 51: 8617-28. PMID 22800196 DOI: 10.1021/Ic3013766 |
0.492 |
|
| 2012 |
Knörzer P, Silakov A, Foster CE, Armstrong FA, Lubitz W, Happe T. Importance of the protein framework for catalytic activity of [FeFe]-hydrogenases Journal of Biological Chemistry. 287: 1489-1499. PMID 22110126 DOI: 10.1074/Jbc.M111.305797 |
0.419 |
|
| 2011 |
Erdem OF, Schwartz L, Stein M, Silakov A, Kaur-Ghumaan S, Huang P, Ott S, Reijerse EJ, Lubitz W. A model of the [FeFe] hydrogenase active site with a biologically relevant azadithiolate bridge: a spectroscopic and theoretical investigation. Angewandte Chemie (International Ed. in English). 50: 1439-43. PMID 21290530 DOI: 10.1002/Anie.201006244 |
0.341 |
|
| 2011 |
Pereira IAC, Matias PM, Shima S, Greco C, Silakov A, Reisner E, Bullock RM. Nickel-Iron-Selenium Hydrogenases - An Overview Structure and Function of [Fe]-Hydrogenase and its Iron-Guanylylpyridinol (FeGP) Cofactor Magnetic Properties of [FeFe]-Hydrogenases: A Theoretical Investigation Based on Extended QM and QM/MM Models of the European Journal of Inorganic Chemistry. 2011: n/a-n/a. DOI: 10.1002/Ejic.201190015 |
0.424 |
|
| 2011 |
Silakov A, Reijerse EJ, Lubitz W. Unraveling the Electronic Properties of the Photoinduced States of the H‐Cluster in the [FeFe] Hydrogenase from D. desulfuricans European Journal of Inorganic Chemistry. 2011: 1056-1066. DOI: 10.1002/Ejic.201001080 |
0.503 |
|
| 2011 |
Greco C, Silakov A, Bruschi M, Ryde U, De Gioia L, Lubitz W. Magnetic properties of [FeFe]-hydrogenases: A theoretical investigation based on extended QM and QM/MM models of the H-cluster and its surroundings European Journal of Inorganic Chemistry. 1043-1049. DOI: 10.1002/Ejic.201001058 |
0.389 |
|
| 2010 |
Silakov A, Shaw JL, Reijerse EJ, Lubitz W. Advanced electron paramagnetic resonance and density functional theory study of a {2Fe3S} cluster mimicking the active site of [FeFe] hydrogenase. Journal of the American Chemical Society. 132: 17578-87. PMID 21082840 DOI: 10.1021/Ja107793E |
0.51 |
|
| 2010 |
Czech I, Silakov A, Lubitz W, Happe T. The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor. Febs Letters. 584: 638-42. PMID 20018187 DOI: 10.1016/J.Febslet.2009.12.016 |
0.483 |
|
| 2009 |
Silakov A, Wenk B, Reijerse E, Lubitz W. (14)N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: evidence for a nitrogen in the dithiol bridge. Physical Chemistry Chemical Physics : Pccp. 11: 6592-9. PMID 19639134 DOI: 10.1039/B905841A |
0.481 |
|
| 2009 |
Silakov A, Kamp C, Reijerse E, Happe T, Lubitz W. Spectroelectrochemical characterization of the active site of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii. Biochemistry. 48: 7780-6. PMID 19634879 DOI: 10.1021/Bi9009105 |
0.532 |
|
| 2009 |
Silakov A, Wenk B, Reijerse E, Albracht SP, Lubitz W. Spin distribution of the H-cluster in the H(ox)-CO state of the [FeFe] hydrogenase from Desulfovibrio desulfuricans: HYSCORE and ENDOR study of (14)N and (13)C nuclear interactions. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 301-13. PMID 19011912 DOI: 10.1007/S00775-008-0449-5 |
0.49 |
|
| 2008 |
Kamp C, Silakov A, Winkler M, Reijerse EJ, Lubitz W, Happe T. Isolation and first EPR characterization of the [FeFe]-hydrogenases from green algae. Biochimica Et Biophysica Acta. 1777: 410-6. PMID 18355437 DOI: 10.1016/J.Bbabio.2008.02.002 |
0.393 |
|
| 2008 |
Abendroth Gv, Stripp S, Silakov A, Croux C, Soucaille P, Girbal L, Happe T. Optimized over-expression of [FeFe] hydrogenases with high specific activity in Clostridium acetobutylicum International Journal of Hydrogen Energy. 33: 6076-6081. DOI: 10.1016/J.Ijhydene.2008.07.122 |
0.39 |
|
| 2007 |
Silakov A, Reijerse EJ, Albracht SP, Hatchikian EC, Lubitz W. The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: a Q-band 57Fe-ENDOR and HYSCORE study. Journal of the American Chemical Society. 129: 11447-58. PMID 17722921 DOI: 10.1021/Ja072592S |
0.439 |
|
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