M. Verkhovsky

发表

Chromophore Photoreduction in Red Fluorescent Proteins Is Responsible for Bleaching and Phototoxicity

Anna I. Krylov, Andreas S. Bommarius, Dmitry A. Bloch, 2014, The journal of physical chemistry. B.

Urocanate reductase: identification of a novel anaerobic respiratory pathway in Shewanella oneidensis MR‐1

D. Bloch, M. Verkhovsky, Y. Bertsova, 2012, Molecular microbiology.

Binding of O(2) and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans.

A. Puustinen, M. Wikström, M. Verkhovsky, 2000, Biochemistry.

Proton translocation by cytochrome c oxidase in different phases of the catalytic cycle.

M. Wikström, M. Verkhovsky, 2002, Biochimica et biophysica acta.

Hidden photoinduced reactivity of the blue fluorescent protein mKalama1.

S. Pletnev, A. Bommarius, Russell B. Vegh, 2015, Physical chemistry chemical physics : PCCP.

Nanosecond electron tunneling between the hemes in cytochrome bo3

Mikael P. Johansson, M. Wikström, M. Verkhovsky, 2007, Proceedings of the National Academy of Sciences.

Oxygen as Acceptor.

M. Verkhovsky, V. Borisov, 2009, EcoSal Plus.

Real-time electron transfer in respiratory complex I

M. Wikström, M. Verkhovsky, L. Euro, 2008, Proceedings of the National Academy of Sciences.

Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I).

M. Wikström, M. Verkhovsky, L. Euro, 2008, Biochimica et biophysica acta.

Intramolecular electron transfer in cytochrome c oxidase: a cascade of equilibria.

M. Wikström, M. Verkhovsky, J. Morgan, 1992, Biochemistry.

Ultrafast haem-haem electron transfer in cytochrome c oxidase.

M. Wikström, M. Verkhovsky, A. Jasaitis, 2001, Biochimica et biophysica acta.

Proton-coupled electron transfer in cytochrome oxidase.

Ville R. I. Kaila, M. Wikström, M. Verkhovsky, 2010, Chemical reviews.

Time-resolved single-turnover of caa(3) oxidase from Thermus thermophilus. Fifth electron of the fully reduced enzyme converts O(H) into E(H) state.

I. Belevich, T. Soulimane, M. Verkhovsky, 2011, Biochimica et biophysica acta.

Kinetic trapping of oxygen in cell respiration

A. Puustinen, M. Wikström, M. Verkhovsky, 1996, Nature.

Proton and electron pathways in the bacterial nitric oxide reductase.

M. Saraste, J. Hendriks, M. Verkhovsky, 2002, Biochemistry.

Sodium-dependent movement of covalently bound FMN residue(s) in Na(+)-translocating NADH:quinone oxidoreductase.

M. Fedin, D. Bloch, M. Verkhovsky, 2012, Biochemistry.

The D-channel of cytochrome oxidase: an alternative view.

M. Wikström, M. Verkhovsky, 2011, Biochimica et biophysica acta.

OXYGEN REDUCTION AND PROTON TRANSLOCATION BY CYTOCHROME C OXIDASE

R. Tuma, M. Verkhovsky, P. Rich, 2009 .

Heme‐copper oxidases with modified D‐ and K‐pathways are yet efficient proton pumps

A. Puustinen, M. Wikström, C. Gomes, 2001, FEBS letters.

Oxygen Reduction and Proton Translocation by the Heme-Copper Oxidases

G. Hummer, M. Wikström, M. Verkhovsky, 1999 .

Perturbation of the CuA site in cytochrome-c oxidase of Paracoccus denitrificans by replacement of Met227 with isoleucine.

M. Wikström, M. Verkhovsky, S. Anemüller, 1995, European journal of biochemistry.

Na+-translocating NADH: Quinone oxidoreductase: Progress achieved and prospects of investigations

M. Verkhovsky, A. Bogachev, 2005, Biochemistry (Moscow).

Prevention of leak in the proton pump of cytochrome c oxidase.

Ville R. I. Kaila, G. Hummer, M. Wikström, 2008, Biochimica et biophysica acta.

Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans.

M. Wikström, M. Verkhovsky, N. Belevich, 2007, Biochemistry.

Towards the mechanism of proton pumping by the haem-copper oxidases.

M. Wikström, M. Verkhovsky, 2006, Biochimica et biophysica acta.

Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen.

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 1999, Biochemistry.

Translocation of electrical charge during a single turnover of cytochrome-c oxidase

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 1997 .

Exploring the proton pump mechanism of cytochrome c oxidase in real time

M. Wikström, I. Belevich, D. Bloch, 2007, Proceedings of the National Academy of Sciences.

pH dependence of proton translocation by Escherichia coli.

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 1992, The Journal of biological chemistry.

Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase.

M. Wikström, M. Verkhovsky, J. Morgan, 1996, Biochemistry.

Proton-coupled electron equilibrium in soluble and membrane-bound cytochrome c oxidase from Paracoccus denitrificans.

M. Wikström, I. Belevich, A. Tuukkanen, 2006, Biochemistry.

Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: a role for protons.

M. Wikström, M. Verkhovsky, J. Morgan, 1995, Biochemistry.

Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy.

K. Vuorilehto, M. Wikström, M. Verkhovsky, 2006, Biochemistry.

An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans.

A. Puustinen, M. Wikström, I. Belevich, 2005, Biochemistry.

Electrogenic events upon photolysis of CO from fully reduced cytochrome c oxidase.

I. Belevich, M. Verkhovsky, Marko Rintanen, 2012, Biochimica et biophysica acta.

Time-resolved OH-->EH transition of the aberrant ba3 oxidase from Thermus thermophilus.

M. Wikström, I. Belevich, T. Soulimane, 2009, Biochimica et biophysica acta.

Elementary steps of proton translocation in the catalytic cycle of cytochrome oxidase.

M. Wikström, I. Belevich, D. Bloch, 2006, Biochimica et biophysica acta.

Role of the PR intermediate in the reaction of cytochrome c oxidase with O2.

M. Wikström, M. Verkhovsky, G. Palmer, 2001, Biochemistry.

Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans.

A. Puustinen, M. Wikström, M. Verkhovsky, 2001, Biochemistry.

Initiation of the proton pump of cytochrome c oxidase

M. Wikström, I. Belevich, M. Verkhovsky, 2010, Proceedings of the National Academy of Sciences.

The "ferrous-oxy" intermediate in the reaction of dioxygen with fully reduced cytochromes aa3 and bo3.

A. Puustinen, M. Wikström, M. Verkhovsky, 1996, Biochemistry.

Elevated proton leak of the intermediate OH in cytochrome c oxidase.

D. Bloch, M. Verkhovsky, A. Jasaitis, 2009, Biophysical journal.

Properties of photosynthetic reaction centers isolated from chromatophores of Chromatium minutissimum

M. Verkhovsky, V. P. Shinkarev, A. Kononenko, 1991 .

Active Site of Cytochrome cbb3*

M. Wikström, D. Bloch, M. Verkhovsky, 2009, Journal of Biological Chemistry.

Intramolecular electron transfer in cytochrome o of Escherichia coli: events following the photolysis of fully and partially reduced CO-bound forms of the bo3 and oo3 enzymes.

A. Puustinen, M. Wikström, M. Verkhovsky, 1993, Biochemistry.

Charge translocation coupled to electron injection into oxidized cytochrome c oxidase from Paracoccus denitrificans.

A. Puustinen, M. Wikström, A. Tuukkanen, 2001, Biochemistry.

The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump.

M. Verkhovsky, M. M. Pereira, M. Verkhovskaya, 2000, Biochemistry.

Heme/heme redox interaction and resolution of individual optical absorption spectra of the hemes in cytochrome bd from Escherichia coli.

D. Bloch, M. Verkhovsky, T. Mogi, 2009, Biochimica et biophysica acta.

Molecular mechanism of proton translocation by cytochrome c oxidase.

I. Belevich, M. Verkhovsky, 2008, Antioxidants & redox signaling.

Proton translocation by cytochrome c oxidase

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 1999, Nature.

Proton and electrical charge translocation by cytochrome-c oxidase

M. Wikström, M. Verkhovsky, J. Morgan, 1997 .

Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase.

M. Wikström, M. Verkhovsky, J. Morgan, 1994, Biochemistry.

A study of the kinetic properties of the stable semiquinone of the reaction-center secondary acceptor in chromatophores of non-sulfur purple bacteria

M. Verkhovsky, V. P. Shinkarev, A. Mulkidjanyan, 1986 .

Tightly-bound ubiquinone in the Escherichia coli respiratory complex I.

D. Bloch, M. Verkhovsky, M. Verkhovskaya, 2012, Biochimica et biophysica acta.

Functioning of quinone acceptors in the reaction center of the green photosynthetic bacterium Chloroflexus aurantiacus

M. Verkhovsky, V. P. Shinkarev, M. Mamedov, 1991, FEBS letters.

The Electrogenic Event Associated with the Reduction of the Secondary Quinone Acceptor in Rhodobacter Sphaeroides Reaction Centers

M. Verkhovsky, V. P. Shinkarev, M. Mamedov, 1990 .

The histidine cycle: A new model for proton translocation in the respiratory heme-copper oxidases

M. Wikström, M. Verkhovsky, J. Morgan, 1994, Journal of bioenergetics and biomembranes.

Sodium-translocating NADH:quinone oxidoreductase as a redox-driven ion pump.

M. Verkhovsky, A. Bogachev, 2010, Biochimica et biophysica acta.

Redox properties of the prosthetic groups of Na(+)-translocating nadh:quinone oxidoreductase. 1. Electron paramagnetic resonance study of the enzyme.

D. Bloch, M. Verkhovsky, L. Kulik, 2009, Biochemistry.

Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase

Ilya Belevich, Mårten Wikström, M. Wikström, 2006, Nature.

The cytochrome bd respiratory oxygen reductases.

R. Gennis, M. Verkhovsky, J. Hemp, 2011, Biochimica et biophysica acta.

The proton donor for OO bond scission by cytochrome c oxidase

M. Wikström, I. Belevich, M. Verkhovsky, 2008, Proceedings of the National Academy of Sciences.

Oxygen as Acceptor

M. Verkhovsky, V. Borisov, 2009, EcoSal Plus.

Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site.

R. Gennis, I. Belevich, M. Verkhovsky, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Discovery of the True Peroxy Intermediate in the Catalytic Cycle of Terminal Oxidases by Real-time Measurement*

I. Belevich, M. Verkhovsky, V. Borisov, 2007, Journal of Biological Chemistry.

Cytochrome bd from Azotobacter vinelandii: evidence for high-affinity oxygen binding.

I. Belevich, D. Bloch, M. Verkhovsky, 2007, Biochemistry.

Electrogenic reactions of cytochrome bd.

M. Verkhovsky, A. Jasaitis, A. A. Konstantinov, 2000, Biochemistry.

Accommodation of CO in the di-heme active site of cytochrome bd terminal oxidase from Escherichia coli.

M. Verkhovsky, V. Borisov, 2013, Journal of inorganic biochemistry.

Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode

Dmitry A. Bloch, Ranjani Murali, Robert B. Gennis, 2011, Proceedings of the National Academy of Sciences.

Glutamate 107 in subunit I of cytochrome bd from Escherichia coli is part of a transmembrane intraprotein pathway conducting protons from the cytoplasm to the heme b595/heme d active site.

I. Belevich, D. Bloch, M. Verkhovsky, 2008, Biochemistry.

Oxygenated complex of cytochrome bd from Escherichia coli: Stability and photolability

I. Belevich, M. Verkhovsky, V. Borisov, 2005, FEBS letters.

Oxygen as Acceptor

M. Verkhovsky, V. Borisov, 2009, EcoSal Plus.

Glutamic acid 242 is a valve in the proton pump of cytochrome c oxidase

Ville R. I. Kaila, G. Hummer, M. Wikström, 2008, Proceedings of the National Academy of Sciences.

The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type.

R. Gennis, A. Puustinen, M. Wikström, 1992, Biochemistry.

The fifth electron in the fully reduced caa(3) from Thermus thermophilus is competent in proton pumping.

M. Wikström, I. Belevich, T. Soulimane, 2013, Biochimica et biophysica acta.

The role of the invariant glutamate 95 in the catalytic site of Complex I from Escherichia coli.

M. Wikström, D. Bloch, M. Verkhovsky, 2009, Biochimica et biophysica acta.

Flash-induced electrogenic events in the photosynthetic reaction center and bc1 complexes of Rhodobacter sphaeroides chromatophores

A. Mulkidjanian, V. Skulachev, M. Verkhovsky, 1989 .

Glutamic acid 286 in subunit I of cytochrome bo3 is involved in proton translocation.

A. Puustinen, M. Wikström, M. Verkhovsky, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Redox properties of the prosthetic groups of Na(+)-translocating NADH:quinone oxidoreductase. 2. Study of the enzyme by optical spectroscopy.

D. Bloch, M. Verkhovsky, Y. Bertsova, 2009, Biochemistry.

Kinetics of the spectral changes during reduction of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi.

M. Wikström, M. Verkhovsky, E. Ruuge, 2002, Biochimica et biophysica acta.

Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi.

B. Barquera, M. Verkhovsky, Y. Bertsova, 2001, Biochemistry.

Probing the mechanistic role of the long α-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis

M. Wikström, M. Verkhovsky, Juho Knuuti, 2011, Molecular microbiology.

Primary Steps of the Na+-translocating NADH:Ubiquinone Oxidoreductase Catalytic Cycle Resolved by the Ultrafast Freeze-Quench Approach*

M. Verkhovsky, Y. Bertsova, A. Bogachev, 2009, Journal of Biological Chemistry.

Site-directed mutagenesis of conserved cysteine residues in NqrD and NqrE subunits of Na+-translocating NADH:quinone oxidoreductase

M. Verkhovsky, Y. Bertsova, A. Bogachev, 2008, Biochemistry (Moscow).

Identification of a "peroxy" intermediate in cytochrome bo3 of Escherichia coli.

A. Puustinen, M. Wikström, M. Verkhovsky, 1995, Biochemistry.

Redox-dependent sodium binding by the Na(+)-translocating NADH:quinone oxidoreductase from Vibrio harveyi.

P. Permi, M. Verkhovsky, Y. Bertsova, 2007, Biochemistry.

Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases.

M. Wikström, M. Verkhovsky, 2007, Biochimica et biophysica acta.

A combined quantum chemical and crystallographic study on the oxidized binuclear center of cytochrome c oxidase.

Ville R. I. Kaila, A. Goldman, M. Wikström, 2011, Biochimica et biophysica acta.

The Protonation State of the Cross-linked Tyrosine during the Catalytic Cycle of Cytochrome c Oxidase*

M. Wikström, M. Verkhovsky, Elena A. Gorbikova, 2008, Journal of Biological Chemistry.

Time-resolved single-turnover of ba3 oxidase from Thermus thermophilus.

M. Wikström, I. Belevich, T. Soulimane, 2007, Biochimica et biophysica acta.

Plasticity of Proton Pathway Structure and Water Coordination in Cytochrome c Oxidase*

M. Verkhovsky, M. Brändén, P. Brzezinski, 2007, Journal of Biological Chemistry.

Water-gated mechanism of proton translocation by cytochrome c oxidase.

G. Hummer, M. Wikström, M. Verkhovsky, 2003, Biochimica et biophysica acta.

The catalytic cycle of cytochrome c oxidase is not the sum of its two halves.

A. Puustinen, M. Wikström, I. Belevich, 2004, Proceedings of the National Academy of Sciences of the United States of America.

The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases.

A. Puustinen, M. Wikström, M. Verkhovsky, 2000, Biochimica et biophysica acta.

Activation of isolated NADH:ubiquinone reductase I (complex I) from Escherichia coli by detergent and phospholipids. Recovery of ubiquinone reductase activity and changes in EPR signals of iron-sulfur clusters.

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 2005, Biochemistry.

Mechanism of proton translocation by the respiratory oxidases. The histidine cycle.

A. Puustinen, M. Finel, M. Wikström, 1994, Biochimica et biophysica acta.

Partial reversion of the electrogenic reaction in the ubiquinol

A. Mulkidjanian, M. Verkhovsky, V. P. Shinkarev, 1990, FEBS Letters.

Effect of pH and surface potential on the rate of electric potential generation due to proton uptake by secondary quinone acceptor of reaction centers in Rhodobacter sphaeroides chromatophores

M. Verkhovsky, V. P. Shinkarev, Armen Mulkidjanian, 1993 .

The K-pathway revisited: a computational study on cytochrome c oxidase.

M. Wikström, A. Tuukkanen, M. Verkhovsky, 2006, Biochimica et biophysica acta.

Redox transitions between oxygen intermediates in cytochrome-c oxidase.

M. Wikström, M. Verkhovsky, M Wikström, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism and energetics by which glutamic acid 242 prevents leaks in cytochrome c oxidase.

Ville R. I. Kaila, G. Hummer, M. Wikström, 2009, Biochimica et biophysica acta.

Gating of proton and water transfer in the respiratory enzyme cytochrome c oxidase.

A. Puustinen, M. Wikström, C. Ribacka, 2005, Proceedings of the National Academy of Sciences of the United States of America.

The calcium binding site in cytochrome aa3 from Paracoccus denitrificans.

A. Puustinen, M. Wikström, M. Verkhovsky, 1999, Biochemistry.

Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor?

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 1999, Biochemistry.

Chapter 4 Electron transfer in respiratory complexes resolved by an ultra-fast freeze-quench approach.

M. Verkhovsky, M. Verkhovskaya, N. Belevich, 2009, Methods in enzymology.

Protolytic reactions on reduction of cytochrome c oxidase studied by ATR-FTIR spectroscopy.

M. Wikström, M. Verkhovsky, N. Belevich, 2007, Biochemistry.

The Na+ and K+ transport deficiency of an E. coli mutant lacking the NhaA and NhaB proteins is apparent and caused by impaired osmoregulation

B. Barquera, M. Wikström, M. Verkhovsky, 1998, FEBS letters.

K+-dependent Na+ transport driven by respiration in Escherichia coli cells and membrane vesicles.

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 1996, Biochimica et biophysica acta.

A novel antiporter activity catalyzing sodium and potassium transport from right‐side‐out vesicles of E. coli

M. Wikström, M. Verkhovsky, M. Verkhovskaya, 1995, FEBS letters.

Interaction between the formyl group of heme a and arginine 54 in cytochrome aa(3) from Paracoccus denitrificans.

A. Puustinen, M. Wikström, M. Verkhovsky, 2000, Biochimica et biophysica acta.

Elevated proton leak of the intermediate OH in cytochrome c oxidase.

D. Bloch, M. Verkhovsky, A. Jasaitis, 2009, Biophysical journal.

Thermodynamic properties of the redox centers of Na(+)-translocating NADH:quinone oxidoreductase.

D. Bloch, M. Verkhovsky, Y. Bertsova, 2006, Biochemistry.