Ahmet S. Vakkasoglu

发表

Cobalt supported on zirconia and sulfated zirconia I.: FT-IR spectroscopic characterization of the NOx species formed upon NO adsorption and NO/O2 coadsorption

M. Kantcheva, Ahmet S. Vakkasoglu, 2004 .

Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter

R. Tampé, R. Gaudet, R. Abele, 2014, Nature Communications.

Peptide-HLA-based immunotherapeutics platforms for direct modulation of antigen-specific T cells

S. Almo, P. Kiener, J. Ross, 2021, Scientific Reports.

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.

R. Gennis, Hyun Ju Lee, P. Brzezinski, 2009, Biochemistry.

Cobalt supported on zirconia and sulfated zirconia II. Reactivity of adsorbed NOx compounds toward methane

M. Kantcheva, Ahmet S. Vakkasoglu, 2004 .

D-VITylation: Harnessing the biology of vitamin D to improve the pharmacokinetic properties of peptides and small proteins.

D. Hall, L. Hales, Ahmet S. Vakkasoglu, 2022, International journal of pharmaceutics.

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.

R. Gennis, P. Brzezinski, Ashtamurthy S Pawate, 2006, Biochemistry.

Water Structural Changes in the L and M Photocycle Intermediates of Bacteriorhodopsin as Revealed by Time-Resolved Step-Scan FTIR Spectroscopy +

R. Gennis, A. Maeda, Ahmet S. Vakkasoglu, 2014 .

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.

R. Gennis, J. Lanyi, A. Maeda, 2010, Biochemistry.

Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286

R. Gennis, Ashtamurthy S Pawate, Ahmet S. Vakkasoglu, 2006, FEBS letters.

Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy.

R. Gennis, A. Maeda, J. Lugtenburg, 2008, Biochemistry.

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.

Jie Zhang, James Hemp, R. Gennis, 2007, Biochemistry.

The 2-methoxy group of ubiquinone is essential for function of the acceptor quinones in reaction centers from Rba. sphaeroides.

C. Wraight, B. Lipshutz, Ahmet S. Vakkasoglu, 2008, Biochimica et Biophysica Acta.

Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.

R. Gennis, J. Lanyi, A. Maeda, 2012, Biophysical journal.

Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus

James Hemp, Robert B. Gennis, James A. Fee, 2012, Proceedings of the National Academy of Sciences.

D-helix influences dimerization of the ATP-binding cassette (ABC) transporter associated with antigen processing 1 (TAP1) nucleotide-binding domain

R. Gaudet, Sriram Srikant, Ahmet S. Vakkasoglu, 2017, PloS one.

Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy.

R. Gennis, A. Maeda, Ahmet S. Vakkasoglu, 2007, Biochemistry.