Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

T G Traylor

Showing results (21-30 of 31) with videos related to

Pageof 4
Sort By:
The Journal of Biological Chemistry|May 5, 1988
Picosecond kinetics of cytochromes b5 and cK A Jongeward, D Magde, D J Taube, et al.
The Journal of Biological Chemistry|November 10, 1977
Reactivity of ferrous myoglobin at low pHG M Giacometti, T G Traylor, P Ascenzi, et al.
Biochemical and Biophysical Research Communications|October 27, 1975
A new method for the determination of ligand dissociation rate constant of carboxyhemoglobinV S Sharma, H M Ranney, J F Geibel, et al.
Biochemistry|March 17, 1992
Reaction of ferrous cytochrome c peroxidase with dioxygen: site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical siteM A Miller, D Bandyopadhyay, J M Mauro, et al.
Biochemical and Biophysical Research Communications|August 31, 1990
Quaternary structure and the geminate recombination of carp hemoglobin with methylisocyanideD Bandyopadhyay, K N Walda, D Magde, et al.
The Journal of Biological Chemistry|October 25, 1983
Reactivity of ferrous heme proteins at low pHT G Traylor, L A Deardurff, M Coletta, et al.
Biochemistry|October 23, 1990
CO dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg 48 influences CO dissociation ratesM A Miller, J M Mauro, G Smulevich, et al.
Biochimica Et Biophysica Acta|March 30, 1972
The vanadium effect in nitrogen fixation by azotobacterJ R Benemann, C E McKenna, R F Lie, et al.
Biochemistry|February 6, 1996
Evidence for a slow tertiary relaxation in the reaction of tert-butyl isocyanide with horseradish peroxidaseD Bandyopadhyay, K N Walda, T M Grogan, et al.
Biochemistry|February 28, 1995
Myoglobin-NO at low pH: free four-coordinated heme in the protein pocketA F Duprat, T G Traylor, G Z Wu, et al.
Pageof 4

Showing results (21-30 of 31) with videos related to

Sort By:
Pageof 4
The Journal of Biological Chemistry|May 5, 1988
Picosecond kinetics of cytochromes b5 and cK A Jongeward, D Magde, D J Taube, et al.
The Journal of Biological Chemistry|November 10, 1977
Reactivity of ferrous myoglobin at low pHG M Giacometti, T G Traylor, P Ascenzi, et al.
Biochemical and Biophysical Research Communications|October 27, 1975
A new method for the determination of ligand dissociation rate constant of carboxyhemoglobinV S Sharma, H M Ranney, J F Geibel, et al.
Biochemistry|March 17, 1992
Reaction of ferrous cytochrome c peroxidase with dioxygen: site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical siteM A Miller, D Bandyopadhyay, J M Mauro, et al.
Biochemical and Biophysical Research Communications|August 31, 1990
Quaternary structure and the geminate recombination of carp hemoglobin with methylisocyanideD Bandyopadhyay, K N Walda, D Magde, et al.
The Journal of Biological Chemistry|October 25, 1983
Reactivity of ferrous heme proteins at low pHT G Traylor, L A Deardurff, M Coletta, et al.
Biochemistry|October 23, 1990
CO dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg 48 influences CO dissociation ratesM A Miller, J M Mauro, G Smulevich, et al.
Biochimica Et Biophysica Acta|March 30, 1972
The vanadium effect in nitrogen fixation by azotobacterJ R Benemann, C E McKenna, R F Lie, et al.
Biochemistry|February 6, 1996
Evidence for a slow tertiary relaxation in the reaction of tert-butyl isocyanide with horseradish peroxidaseD Bandyopadhyay, K N Walda, T M Grogan, et al.
Biochemistry|February 28, 1995
Myoglobin-NO at low pH: free four-coordinated heme in the protein pocketA F Duprat, T G Traylor, G Z Wu, et al.
Pageof 4