Year |
Citation |
Score |
2017 |
von Ballmoos C, Smirnova I, Poiana F, Gonska N, Chang H, Gennis RB, Brzezinski P, Ädelroth P. Dynamics of the KBProton Pathway in Cytochromeba3fromThermus thermophilus Israel Journal of Chemistry. 57: 424-436. DOI: 10.1002/Ijch.201600136 |
0.646 |
|
2013 |
Smirnova I, Chang HY, von Ballmoos C, Ädelroth P, Gennis RB, Brzezinski P. Single mutations that redirect internal proton transfer in the ba3 oxidase from Thermus thermophilus. Biochemistry. 52: 7022-30. PMID 24004023 DOI: 10.1021/Bi4008726 |
0.577 |
|
2012 |
Chang HY, Choi SK, Vakkasoglu AS, Chen Y, Hemp J, Fee JA, Gennis RB. Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus. Proceedings of the National Academy of Sciences of the United States of America. 109: 5259-64. PMID 22431640 DOI: 10.1073/Pnas.1107345109 |
0.615 |
|
2012 |
Chang H, Choi S, Vakkasoglu A, Chen Y, Hemp J, Fee J, Gennis R. Investigation of the proton pump and exit pathway in cytochrome ba3 from Thermus thermophilus Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S106. DOI: 10.1016/J.Bbabio.2012.06.286 |
0.607 |
|
2010 |
Chang HY, Ahn Y, Pace LA, Lin MT, Lin YH, Gennis RB. The diheme cytochrome c(4) from Vibrio cholerae is a natural electron donor to the respiratory cbb(3) oxygen reductase. Biochemistry. 49: 7494-503. PMID 20715760 DOI: 10.1021/Bi1004574 |
0.576 |
|
2010 |
Smirnova I, Reimann J, von Ballmoos C, Chang HY, Gennis RB, Fee JA, Brzezinski P, Adelroth P. Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus. Biochemistry. 49: 7033-9. PMID 20677778 DOI: 10.1021/Bi100749P |
0.526 |
|
2009 |
Chang HY, Hemp J, Chen Y, Fee JA, Gennis RB. The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping. Proceedings of the National Academy of Sciences of the United States of America. 106: 16169-73. PMID 19805275 DOI: 10.1073/Pnas.0905264106 |
0.548 |
|
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