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FEBS Letters
|
August 15, 1976
Accelerated catalysis by active succinate dehydrogenase: a reflection of a novel regulatory site
A Gopher, M Gutman
European Journal of Biochemistry
|
November 1, 1975
Characterization of the component, which controls the transformation between the kinetic forms of the b cytochromes
M Eisenbach, M Gutman
Annual Review of Physical Chemistry
|
January 1, 1997
Time-resolved dynamics of proton transfer in proteinous systems
M Gutman, E Nachliel
FEBS Letters
|
September 16, 1996
Quantitative evaluation of the dynamics of proton transfer from photoactivated bacteriorhodopsin to the bulk
E Nachliel, M Gutman
Biochimica Et Biophysica Acta
|
March 15, 1977
Distinction between NAD- and NADH-binding forms of mitochondrial malate dehydrogenase as shown by inhibition with thenoyltrifuoroacetone
M Gutman, E Hartstein
Molecular and Cellular Biochemistry
|
April 30, 1975
The steady state activity of succinate dehydrogenase in the presence of opposing effectors. 1. The effect of L malate and CoQH2 on the enzymic activity
M Gutman, N Silamn
Israel Journal of Medical Sciences
|
November 1, 1975
Proceedings: Novel mechanism affecting the catalytic activity of mitochondrial succinate dehydrogenase
A Gopher, M Gutman
Biochemistry
|
June 4, 1985
Kinetic analysis of protonation of a specific site on a buffered surface of a macromolecular body
M Gutman, E Nachliel
FEBS Letters
|
September 1, 1976
Mechanism of inhibition by ubicidin: inhibitor with piericidin ring structure and ubiquinone side chain
M Gutman, S Kliatchko
FEBS Letters
|
January 15, 1976
Demonstration of the active and the sluggish forms of cytochrome b in isolated b-c1 complexes of the respiratory chain
M Eisenbach, M Gutman
Page
of 28
Search research articles
Search
Showing results (21-30 of 279) with videos related to
Sort By:
Page
of 28
FEBS Letters
|
August 15, 1976
Accelerated catalysis by active succinate dehydrogenase: a reflection of a novel regulatory site
A Gopher, M Gutman
European Journal of Biochemistry
|
November 1, 1975
Characterization of the component, which controls the transformation between the kinetic forms of the b cytochromes
M Eisenbach, M Gutman
Annual Review of Physical Chemistry
|
January 1, 1997
Time-resolved dynamics of proton transfer in proteinous systems
M Gutman, E Nachliel
FEBS Letters
|
September 16, 1996
Quantitative evaluation of the dynamics of proton transfer from photoactivated bacteriorhodopsin to the bulk
E Nachliel, M Gutman
Biochimica Et Biophysica Acta
|
March 15, 1977
Distinction between NAD- and NADH-binding forms of mitochondrial malate dehydrogenase as shown by inhibition with thenoyltrifuoroacetone
M Gutman, E Hartstein
Molecular and Cellular Biochemistry
|
April 30, 1975
The steady state activity of succinate dehydrogenase in the presence of opposing effectors. 1. The effect of L malate and CoQH2 on the enzymic activity
M Gutman, N Silamn
Israel Journal of Medical Sciences
|
November 1, 1975
Proceedings: Novel mechanism affecting the catalytic activity of mitochondrial succinate dehydrogenase
A Gopher, M Gutman
Biochemistry
|
June 4, 1985
Kinetic analysis of protonation of a specific site on a buffered surface of a macromolecular body
M Gutman, E Nachliel
FEBS Letters
|
September 1, 1976
Mechanism of inhibition by ubicidin: inhibitor with piericidin ring structure and ubiquinone side chain
M Gutman, S Kliatchko
FEBS Letters
|
January 15, 1976
Demonstration of the active and the sluggish forms of cytochrome b in isolated b-c1 complexes of the respiratory chain
M Eisenbach, M Gutman
Page
of 28