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J T Hazzard

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Biochemistry|June 3, 1986
Kinetic studies of reduction of a 1:1 cytochrome c-flavodoxin complex by free flavin semiquinones and rubredoxinJ T Hazzard, M A Cusanovich, J A Tainer, et al.
Biochemistry|March 22, 1988
Kinetics of intracomplex electron transfer and of reduction of the components of covalent and noncovalent complexes of cytochrome c and cytochrome c peroxidase by free flavin semiquinonesJ T Hazzard, S J Moench, J E Erman, et al.
Biochemistry|June 14, 1988
Effects of amino acid replacements in yeast iso-1 cytochrome c on heme accessibility and intracomplex electron transfer in complexes with cytochrome c peroxidaseJ T Hazzard, G McLendon, M A Cusanovich, et al.
Biochemistry|September 24, 1991
Unimolecular and bimolecular oxidoreduction reactions involving diprotein complexes of cytochrome c and plastocyanin. Dependence of electron-transfer reactivity on charge and orientation of the docked metalloproteinsL M Peerey, H M Brothers, J T Hazzard, et al.
Protein Science : a Publication of the Protein Society|August 19, 1999
Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NADP+ reductase: site-specific mutagenesis, transient kinetic measurements, and electrostatic surface potentialsJ K Hurley, J T Hazzard, M Martínez-Júlvez, et al.
Biochemistry|November 15, 2000
Highly nonproductive complexes with Anabaena ferredoxin at low ionic strength are induced by nonconservative amino acid substitutions at Glu139 in Anabaena ferredoxin:NADP+ reductaseJ K Hurley, M Faro, T B Brodie, et al.
Biochemistry|August 23, 1988
Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidationJ M Mauro, L A Fishel, J T Hazzard, et al.
Biochemistry|December 27, 1988
Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome cM A Miller, J T Hazzard, J M Mauro, et al.
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Showing results (21-30 of 28) with videos related to

Sort By:
Pageof 3
You have reached the last page of results.This site can display upto 28 results.
Biochemistry|June 3, 1986
Kinetic studies of reduction of a 1:1 cytochrome c-flavodoxin complex by free flavin semiquinones and rubredoxinJ T Hazzard, M A Cusanovich, J A Tainer, et al.
Biochemistry|March 22, 1988
Kinetics of intracomplex electron transfer and of reduction of the components of covalent and noncovalent complexes of cytochrome c and cytochrome c peroxidase by free flavin semiquinonesJ T Hazzard, S J Moench, J E Erman, et al.
Biochemistry|June 14, 1988
Effects of amino acid replacements in yeast iso-1 cytochrome c on heme accessibility and intracomplex electron transfer in complexes with cytochrome c peroxidaseJ T Hazzard, G McLendon, M A Cusanovich, et al.
Biochemistry|September 24, 1991
Unimolecular and bimolecular oxidoreduction reactions involving diprotein complexes of cytochrome c and plastocyanin. Dependence of electron-transfer reactivity on charge and orientation of the docked metalloproteinsL M Peerey, H M Brothers, J T Hazzard, et al.
Protein Science : a Publication of the Protein Society|August 19, 1999
Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NADP+ reductase: site-specific mutagenesis, transient kinetic measurements, and electrostatic surface potentialsJ K Hurley, J T Hazzard, M Martínez-Júlvez, et al.
Biochemistry|November 15, 2000
Highly nonproductive complexes with Anabaena ferredoxin at low ionic strength are induced by nonconservative amino acid substitutions at Glu139 in Anabaena ferredoxin:NADP+ reductaseJ K Hurley, M Faro, T B Brodie, et al.
Biochemistry|August 23, 1988
Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidationJ M Mauro, L A Fishel, J T Hazzard, et al.
Biochemistry|December 27, 1988
Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome cM A Miller, J T Hazzard, J M Mauro, et al.
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