Year |
Citation |
Score |
2018 |
Maklashina E, Rajagukguk S, Iverson TM, Cecchini G. The unassembled flavoprotein subunits of human and bacterial complex II have impaired catalytic activity and generate only minor amounts of ROS. The Journal of Biological Chemistry. 293: 7754-7765. PMID 29610278 DOI: 10.1074/Jbc.Ra118.001977 |
0.433 |
|
2016 |
Starbird C, Maklashina E, Rajagukguk S, Cecchini G, Iverson T. Mechanisms of Assembly and Covalent Flavinylation in Complex II Biophysical Journal. 110: 191a. DOI: 10.1016/J.Bpj.2015.11.1065 |
0.417 |
|
2016 |
Maklashina E, Rajagukguk S, Cecchini G. Catalytic properties of the flavoprotein subunit of Complex II Biochimica Et Biophysica Acta. 1857. DOI: 10.1016/J.Bbabio.2016.04.306 |
0.353 |
|
2015 |
Maklashina E, Rajagukguk S, Starbird CA, McDonald WH, Koganitsky A, Eisenbach M, Iverson TM, Cecchini G. Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II. The Journal of Biological Chemistry. PMID 26644464 DOI: 10.1074/Jbc.M115.690396 |
0.41 |
|
2014 |
Anderson RF, Shinde SS, Hille R, Rothery RA, Weiner JH, Rajagukguk S, Maklashina E, Cecchini G. Electron-transfer pathways in the heme and quinone-binding domain of complex II (succinate dehydrogenase). Biochemistry. 53: 1637-46. PMID 24559074 DOI: 10.1021/Bi401630M |
0.549 |
|
2013 |
Singh PK, Sarwar M, Maklashina E, Kotlyar V, Rajagukguk S, Tomasiak TM, Cecchini G, Iverson TM. Plasticity of the quinone-binding site of the complex II homolog quinol:fumarate reductase. The Journal of Biological Chemistry. 288: 24293-301. PMID 23836905 DOI: 10.1074/Jbc.M113.487082 |
0.452 |
|
2013 |
Millett F, Havens J, Rajagukguk S, Durham B. Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c. Biochimica Et Biophysica Acta. 1827: 1309-19. PMID 22985600 DOI: 10.1016/J.Bbabio.2012.09.002 |
0.687 |
|
2010 |
Maklashina E, Rajagukguk S, McIntire WS, Cecchini G. Mutation of the heme axial ligand of Escherichia coli succinate-quinone reductase: implications for heme ligation in mitochondrial complex II from yeast. Biochimica Et Biophysica Acta. 1797: 747-754. PMID 20100456 DOI: 10.1016/J.Bbabio.2010.01.019 |
0.493 |
|
2008 |
Millett F, Brand SE, Rajagukguk S, Ganesan K, Geren L, Fabian M, Han D, Gennis RB, Durham B, Ferguson-Miller S, Mills DA. C2/2 Rapid kinetic studies of electron transfer in cytochrome oxidase Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S109. DOI: 10.1016/J.Bbabio.2008.05.428 |
0.657 |
|
2007 |
Brand SE, Rajagukguk S, Ganesan K, Geren L, Fabian M, Han D, Gennis RB, Durham B, Millett F. A new ruthenium complex to study single-electron reduction of the pulsed O(H) state of detergent-solubilized cytochrome oxidase. Biochemistry. 46: 14610-8. PMID 18027981 DOI: 10.1021/Bi701424D |
0.553 |
|
2007 |
Rajagukguk S, Yang S, Yu CA, Yu L, Durham B, Millett F. Effect of mutations in the cytochrome b ef loop on the electron-transfer reactions of the Rieske iron-sulfur protein in the cytochrome bc1 complex. Biochemistry. 46: 1791-8. PMID 17253777 DOI: 10.1021/Bi062094G |
0.54 |
|
2004 |
Zaslavsky D, Sadoski RC, Rajagukguk S, Geren L, Millett F, Durham B, Gennis RB. Direct measurement of proton release by cytochrome c oxidase in solution during the F-->O transition. Proceedings of the National Academy of Sciences of the United States of America. 101: 10544-7. PMID 15247424 DOI: 10.1073/Pnas.0401521101 |
0.494 |
|
2003 |
Xiao K, Engstrom G, Rajagukguk S, Yu CA, Yu L, Durham B, Millett F. Effect of famoxadone on photoinduced electron transfer between the iron-sulfur center and cytochrome c1 in the cytochrome bc1 complex. The Journal of Biological Chemistry. 278: 11419-26. PMID 12525495 DOI: 10.1074/Jbc.M211620200 |
0.616 |
|
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