P. Adelroth

发表

Inhibition of proton pumping by zinc ions during specific reaction steps in cytochrome c oxidase.

P. Brzezinski, Kristina Faxén, Lina Salomonsson, 2006, Biochimica et biophysica acta.

Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors.

G. Feher, M. Okamura, A. Tehrani, 2001, Biochemistry.

Glutamate 286 in cytochrome aa3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen.

R. Gennis, P. Brzezinski, P. Adelroth, 1997, Biochemistry.

Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase.

R. Gennis, P. Brzezinski, P. Adelroth, 2000, Biochimica et biophysica acta.

Molecular architecture of the proton diode of cytochrome c oxidase.

P. Brzezinski, J. Reimann, P. Adelroth, 2008, Biochemical Society transactions.

Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer.

P. Brzezinski, P. Adelroth, M. Karpefors, 2000, Biochemistry.

Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides.

P. Brzezinski, B. Malmström, P. Adelroth, 1995, Biochemistry.

Proton transfer in ba(3) cytochrome c oxidase from Thermus thermophilus.

R. Gennis, P. Brzezinski, C. von Ballmoos, 2012, Biochimica et biophysica acta.

Studies of Ca2+ binding in spinach photosystem II using 45Ca2+.

P. Adelroth, L. Andréasson, K. Lindberg, 1995, Biochemistry.

Studies of Ca2+ binding in spinach photosystem II using 45Ca2+.

P. Adelroth, L. Andréasson, K. Lindberg, 1994, Biochemical Society transactions.

Proton transfer in the quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus during reduction of oxygen.

J. Reimann, Y. Shiro, T. Tosha, 2012, Biochimica et biophysica acta.

Electron/proton coupling in bacterial nitric oxide reductase during reduction of oxygen.

P. Adelroth, N. Watmough, U. Flock, 2005, Biochemistry.

Substrate binding and the catalytic reactions in cbb3-type oxidases: the lipid membrane modulates ligand binding.

Yafei Huang, J. Reimann, P. Adelroth, 2010, Biochimica et biophysica acta.

Identification of the proton pathway in bacterial reaction centers: cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (QB).

G. Feher, M. Okamura, E. Abresch, 2001, Biochemistry.

Functional proton transfer pathways in the heme-copper oxidase superfamily.

Hyun Ju Lee, Yafei Huang, J. Reimann, 2012, Biochimica et biophysica acta.

Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme.

P. Brzezinski, P. Adelroth, M. Ek, 1998, Biochimica et biophysica acta.

Intermediates generated during the reaction of reduced Rhodobacter sphaeroides cytochrome c oxidase with dioxygen.

P. Brzezinski, P. Adelroth, L. Ojemyr, 2013, Biochimica et biophysica acta.

Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation.

R. Gennis, P. Brzezinski, P. Adelroth, 1999, Biochemistry.

Site-directed mutagenesis of residues lining a putative proton transfer pathway in cytochrome c oxidase from Rhodobacter sphaeroides.

R. Gennis, Y. Kim, S. Ferguson-Miller, 1996, Biochemistry.

Kinetic coupling between electron and proton transfer in cytochrome c oxidase: simultaneous measurements of conductance and absorbance changes.

P. Brzezinski, P. Adelroth, S. Hallén, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Triplet-state quenching in complexes between Zn-cytochrome c and cytochrome oxidase or its CuA domain.

M. Wilson, P. Brzezinski, M. Sundahl, 1995, Biophysical chemistry.

Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus.

R. Gennis, P. Brzezinski, J. Reimann, 2010, Biochemistry.

Localized control of proton transfer through the D-pathway in cytochrome c oxidase: application of the proton-inventory technique.

P. Brzezinski, P. Adelroth, M. Karpefors, 2000, Biochemistry.

The onset of the deuterium isotope effect in cytochrome c oxidase.

P. Brzezinski, P. Adelroth, M. Karpefors, 2000, Biochemistry.

Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides.

R. Gennis, P. Brzezinski, P. Adelroth, 1998, Biochemistry.

Factors determining electron-transfer rates in cytochrome c oxidase: studies of the FQ(I-391) mutant of the Rhodobacter sphaeroides enzyme.

R. Gennis, P. Brzezinski, P. Adelroth, 1997, Biochemistry.

Surface proton donors for the D-pathway of cytochrome c oxidase in the absence of subunit III.

P. Adelroth, J. Hosler, 2006, Biochemistry.

Observation of a novel transient ferryl complex with reduced CuB in cytochrome c oxidase.

R. Gennis, P. Brzezinski, P. Adelroth, 1999, Biochemistry.

EPR studies of wild‐type and several mutants of cytochrome c oxidase from Rhodobacter sphaeroides: Glu286 is not a bridging ligand in the cytochrome a 3‐CuB center

R. Gennis, P. Brzezinski, B. Malmström, 1995, FEBS letters.

Surface-mediated proton-transfer reactions in membrane-bound proteins.

P. Brzezinski, P. Adelroth, 2004, Biochimica et biophysica acta.

Special issue on proton transfer in biological systems.

P. Adelroth, 2006, Biochimica et biophysica acta.

The timing of proton migration in membrane-reconstituted cytochrome c oxidase.

P. Brzezinski, Kristina Faxén, Lina Salomonsson, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Kinetics of electron and proton transfer during O(2) reduction in cytochrome aa(3) from A. ambivalens: an enzyme lacking Glu(I-286).

C. Gomes, P. Brzezinski, M. Teixeira, 2001, Biochimica et biophysica acta.

Design principles of proton-pumping haem-copper oxidases.

P. Brzezinski, P. Adelroth, 2006, Current opinion in structural biology.

Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase.

P. Lachmann, J. Reimann, P. Adelroth, 2009, Journal of inorganic biochemistry.

A pathway for protons in nitric oxide reductase from Paracoccus denitrificans.

J. Reimann, A. Honigmann, P. Adelroth, 2007, Biochimica et biophysica acta.

Proton uptake controls electron transfer in cytochrome c oxidase.

S. Ferguson-Miller, P. Brzezinski, P. Adelroth, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Electron-proton interactions in terminal oxidases.

P. Brzezinski, A. Aagaard, P. Adelroth, 1998, Biochimica et biophysica acta.

Determination of proton transfer rates by chemical rescue: application to bacterial reaction centers.

G. Feher, M. Okamura, J. Beatty, 2002, Biochemistry.

Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry point.

G. Feher, M. Okamura, M. Paddock, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Functional proton transfer pathways in the heme-copper oxidase superfamily.

Hyun Ju Lee, Yafei Huang, J. Reimann, 2012, Biochimica et biophysica acta.

Studies of Ca * + binding in spinach Photosystem II using 45 Ca 2 +

P. Adelroth, L. Andréasson, K. Lindberg, 2022 .