Ahmet S. Vakkasoglu, Ph.D.

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
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"Ahmet Vakkasoglu"
Mean distance: 9.67
 
SNBCP

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Robert B. Gennis grad student 2008 UIUC
 (FTIR difference spectroscopy studies on membrane proteins.)
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Publications

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Grossmann N, Vakkasoglu AS, Hulpke S, et al. (2014) Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter. Nature Communications. 5: 5419
Morgan JE, Vakkasoglu AS, Lanyi JK, et al. (2012) Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle. Biophysical Journal. 103: 444-52
Chang HY, Choi SK, Vakkasoglu AS, et al. (2012) 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
Morgan JE, Vakkasoglu AS, Lanyi JK, et al. (2010) 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
Lee HJ, Ojemyr L, Vakkasoglu A, et al. (2009) 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
Morgan JE, Vakkasoglu AS, Lugtenburg J, et al. (2008) 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
Wraight CA, Vakkasoglu AS, Poluektov Y, et al. (2008) 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
Yang K, Zhang J, Vakkasoglu AS, et al. (2007) 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
Morgan JE, Vakkasoglu AS, Gennis RB, et al. (2007) 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
Han D, Namslauer A, Pawate A, et al. (2006) 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
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