Ahmet S. Vakkasoglu, Ph.D. - Publications

Affiliations: 
2008 University of Illinois, Urbana-Champaign, Urbana-Champaign, IL 
Area:
Membrane protein structure/function; Expression of membrane proteins from hyperthermophiles; Structure and mechanism of prokaryotic respiratory enzymes that generate a membrane potential

13 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2014 Grossmann N, Vakkasoglu AS, Hulpke S, Abele R, Gaudet R, Tampé R. Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter. Nature Communications. 5: 5419. PMID 25377891 DOI: 10.1038/Ncomms6419  0.72
2012 Morgan JE, Vakkasoglu AS, Lanyi JK, Lugtenburg J, Gennis RB, Maeda A. Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle. Biophysical Journal. 103: 444-52. PMID 22947860 DOI: 10.1016/J.Bpj.2012.06.022  0.72
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  0.72
2010 Morgan JE, Vakkasoglu AS, Lanyi JK, Gennis RB, Maeda A. Coordinating the structural rearrangements associated with unidirectional proton transfer in the bacteriorhodopsin photocycle induced by deprotonation of the proton-release group: a time-resolved difference FTIR spectroscopic study. Biochemistry. 49: 3273-81. PMID 20232848 DOI: 10.1021/Bi901757Y  0.72
2009 Lee HJ, Ojemyr L, Vakkasoglu A, Brzezinski P, Gennis RB. Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump. Biochemistry. 48: 7123-31. PMID 19575527 DOI: 10.1021/Bi901015D  0.72
2008 Morgan JE, Vakkasoglu AS, Lugtenburg J, Gennis RB, Maeda A. Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy. Biochemistry. 47: 11598-605. PMID 18837559 DOI: 10.1021/Bi801405V  0.72
2008 Wraight CA, Vakkasoglu AS, Poluektov Y, Mattis AJ, Nihan D, Lipshutz BH. The 2-methoxy group of ubiquinone is essential for function of the acceptor quinones in reaction centers from Rba. sphaeroides. Biochimica Et Biophysica Acta. 1777: 631-6. PMID 18474215 DOI: 10.1016/J.Bbabio.2008.04.025  0.72
2007 Yang K, Zhang J, Vakkasoglu AS, Hielscher R, Osborne JP, Hemp J, Miyoshi H, Hellwig P, Gennis RB. Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center. Biochemistry. 46: 3270-8. PMID 17305364 DOI: 10.1021/Bi061946+  0.72
2007 Morgan JE, Vakkasoglu AS, Gennis RB, Maeda A. Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy. Biochemistry. 46: 2787-96. PMID 17300175 DOI: 10.1021/Bi0616596  0.72
2006 Han D, Namslauer A, Pawate A, Morgan JE, Nagy S, Vakkasoglu AS, Brzezinski P, Gennis RB. Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump. Biochemistry. 45: 14064-74. PMID 17115701 DOI: 10.1021/Bi061465Q  0.72
2006 Vakkasoglu AS, Morgan JE, Han D, Pawate AS, Gennis RB. Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286. Febs Letters. 580: 4613-7. PMID 16890226 DOI: 10.1016/J.Febslet.2006.07.036  0.72
2004 Kantcheva M, Vakkasoglu AS. Cobalt supported on zirconia and sulfated zirconia I. FT-IR spectroscopic characterization of the NOx species formed upon NO adsorption and NO/O2 coadsorption Journal of Catalysis. 223: 352-363. DOI: 10.1016/J.Jcat.2004.02.007  0.72
2004 Kantcheva M, Vakkasoglu AS. Cobalt supported on zirconia and sulfated zirconia: II. Reactivity of adsorbed NOx compounds toward methane Journal of Catalysis. 223: 364-371. DOI: 10.1016/J.Jcat.2004.02.006  0.72
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