G B Postnikova - JoVE Visualize

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European Journal of Biochemistry|May 15, 1985

Spin-label study of conformational changes induced by pH and ligands in leghemoglobin from yellow lupine root nodulesG B Postnikova, E M Yumakova, E S Yakovleva

Biofizika|November 1, 1996

[Electron transfer in hemoproteins. The applicability of models of electrostatic interaction of molecules for description of the relationship between the myoglobin and cytochrome reaction rate and the ionic strength]V S Sivozhelezov, Iu E Komarov, G B Postnikova

Inorganic Chemistry|January 22, 2010

The main role of inner histidines in the molecular mechanism of myoglobin oxidation catalyzed by copper compoundsG B Postnikova, S A Moiseeva, E A Shekhovtsova

Biofizika|July 14, 2001

[Catalytic effect of ferricyanide on the rate of electron transfer between myoglobin and cytochrome c]S A Moiseeva, G B Postnikova, V S Sivozhelezov

Biophysical Chemistry|April 1, 1983

A spin label study of conformational changes in cytochrome cG B Postnikova, N P Gorbunova, M V Volkenstein

Molekuliarnaia Biologiia|January 1, 1984

[Electron transport in hemoproteins. VIII. The effect of chemical modification of ferricytochrome C on the rate of its reduction by oxymyoglobin]G B Postnikova, N P Gorbunova, B P Atanasov

Biofizika|January 13, 2001

[Oxidation of sperm whale oxymyoglobin, catalyzed by ferrocyanide ions: kinetics and mechanisms]S A Moiseeva, G B Postnikova, V S Sivozhelezov

European Journal of Biochemistry|May 23, 1991

Fluorescence study of the conformational properties of myoglobin structure. 1. pH-dependent changes of tryptophanyl fluorescence in intact and chemically modified sperm whale apomyoglobinsG B Postnikova, Y E Komarov, E M Yumakova

Biokhimiia (Moscow, Russia)|February 1, 1986

[pH-dependent changes in the tryptophan and porphyrin fluorescence of the apomyoglobin complex with protoporphyrin IX and methemoglobin]G B Postnikova, E M Iumakova, N L Vekshin

Molekuliarnaia Biologiia|January 1, 1982

[Electron transfer in hemoproteins. VIII. Influence of ionic strength on the rate of reduction of ferricytochrome c by oxymyoglobin derivatives, chemically modified at histidine residues]G B Postnikova, E A Shliapnikova, B P Atanasov, et al.

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Showing results (21-30 of 40) with videos related to

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European Journal of Biochemistry|May 15, 1985

Spin-label study of conformational changes induced by pH and ligands in leghemoglobin from yellow lupine root nodulesG B Postnikova, E M Yumakova, E S Yakovleva

Biofizika|November 1, 1996

[Electron transfer in hemoproteins. The applicability of models of electrostatic interaction of molecules for description of the relationship between the myoglobin and cytochrome reaction rate and the ionic strength]V S Sivozhelezov, Iu E Komarov, G B Postnikova

Inorganic Chemistry|January 22, 2010

The main role of inner histidines in the molecular mechanism of myoglobin oxidation catalyzed by copper compoundsG B Postnikova, S A Moiseeva, E A Shekhovtsova

Biofizika|July 14, 2001

[Catalytic effect of ferricyanide on the rate of electron transfer between myoglobin and cytochrome c]S A Moiseeva, G B Postnikova, V S Sivozhelezov

Biophysical Chemistry|April 1, 1983

A spin label study of conformational changes in cytochrome cG B Postnikova, N P Gorbunova, M V Volkenstein

Molekuliarnaia Biologiia|January 1, 1984

[Electron transport in hemoproteins. VIII. The effect of chemical modification of ferricytochrome C on the rate of its reduction by oxymyoglobin]G B Postnikova, N P Gorbunova, B P Atanasov

Biofizika|January 13, 2001

[Oxidation of sperm whale oxymyoglobin, catalyzed by ferrocyanide ions: kinetics and mechanisms]S A Moiseeva, G B Postnikova, V S Sivozhelezov

European Journal of Biochemistry|May 23, 1991

Fluorescence study of the conformational properties of myoglobin structure. 1. pH-dependent changes of tryptophanyl fluorescence in intact and chemically modified sperm whale apomyoglobinsG B Postnikova, Y E Komarov, E M Yumakova

Biokhimiia (Moscow, Russia)|February 1, 1986

[pH-dependent changes in the tryptophan and porphyrin fluorescence of the apomyoglobin complex with protoporphyrin IX and methemoglobin]G B Postnikova, E M Iumakova, N L Vekshin

Molekuliarnaia Biologiia|January 1, 1982

[Electron transfer in hemoproteins. VIII. Influence of ionic strength on the rate of reduction of ferricytochrome c by oxymyoglobin derivatives, chemically modified at histidine residues]G B Postnikova, E A Shliapnikova, B P Atanasov, et al.

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