D. Bloch

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.

A single amino acid residue controls ROS production in the respiratory Complex I from Escherichia coli

Vivek Sharma, D. Bloch, Juho Knuuti, 2013, Molecular microbiology.

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

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

Hidden photoinduced reactivity of the blue fluorescent protein mKalama1.

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

Flash‐induced electrogenic reactions in the SA(L223) reaction center mutant in Rhodobacter sphaeroides chromatophores

D. Oesterhelt, D. Bloch, D. Cherepanov, 1994, FEBS letters.

6-Ketocholestanol is a recoupler for mitochondria, chromatophores and cytochrome oxidase proteoliposomes.

V. Skulachev, D. Bloch, A. Starkov, 1997, Biochimica et biophysica acta.

Some male sex hormones, progesterone and 6-ketocholestanol counteract uncoupling effects of low concentrations of the most active protonophores*

V. Skulachev, D. Bloch, A. Starkov, 1995 .

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

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

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.

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.

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

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

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

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

Active Site of Cytochrome cbb3*

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

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.

Energy-converting respiratory Complex I: on the way to the molecular mechanism of the proton pump.

D. Bloch, M. Verkhovskaya, 2013, The international journal of biochemistry & cell biology.

Pumping capacity of bacterial reaction centers and backpressure regulation of energy transduction.

R. W. Visschers, H. Westerhoff, M. Jones, 2001, European journal of biochemistry.

Effect of temperature and surface potential on the electrogenic proton uptake in the QB site of the Rhodobacter sphaeroides photosynthetic reaction center: QA−.B−. → QAQBH2 transition

A. Mulkidjanian, D. Bloch, D. Cherepanov, 1998, Photosynthesis Research.

Reduction and protonation of the secondary quinone acceptor of Rhodobacter sphaeroides photosynthetic reaction center: kinetic model based on a comparison of wild-type chromatophores with mutants carrying Arg-->Ile substitution at sites 207 and 217 in the L-subunit.

D. Oesterhelt, A. Mulkidjanian, D. Bloch, 2000, Biochimica et biophysica acta.

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

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

Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q10 substitution by decylubiquinone in the QB binding site

D. Bloch, A. Semenov, Oxana A Gopta, 2001, FEBS letters.

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.

Energetics of alkalophilic representatives of the genus Bacillus

D. Bloch, V. Ustiyan, E. Skripnikova, 2005, Biochemistry (Moscow).

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

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

Cytochrome cbb3 of Thioalkalivibrio is a Na+-pumping cytochrome oxidase

R. Lahti, G. Muyzer, V. Skulachev, 2015, Proceedings of the National Academy of Sciences.

Kinetics of CO binding to H+‐motive oxidases of the caa 3‐type from Bacillus FTU and of the o‐type from Escherichia coli

D. Bloch, M. Muntyan, L.A. Drachev, 1993, FEBS letters.

Study of redox potential in cytochrome c covalently bound to terminal oxidase of alkaliphilic Bacillus pseudofirmus FTU

D. Bloch, M. Muntyan, 2008, Biochemistry (Moscow).

Kinetics of CO binding to putative Na+‐motive oxidases of the o‐type from Bacillus FTU and of the d‐type from Escherichia coli

V. Skulachev, D. Bloch, M. Muntyan, 1993, FEBS letters.

Mechanistic stoichiometry of proton translocation by cytochrome cbb3

M. Wikström, D. Bloch, V. Rauhamäki, 2012, Proceedings of the National Academy of Sciences.

Study of redox potential in cytochrome c covalently bound to terminal oxidase of alkaliphilic Bacillus pseudofirmus FTU

D. Bloch, M. Muntyan, 2008 .

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.

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.

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 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.

Electrogenic Reactions in the High-Potential Segment of the Cytochrome bc1 — Complex

D. Bloch, A. Semenov, O. Gopta, 1995 .

Electrogenic events in chromatophores fromRhodobacter sphaeroides lacking high-potential cytochrome b of thebc1-complex

A. Crofts, C. Yun, R. Gennis, 1992 .

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

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

Two o-type oxidases in Methylobacillus flagellatum KT.

A. Netrusov, D. Bloch, T. Y. Dinarieva, 1994, Biochemical and biophysical research communications.

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

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