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

Victor L Davidson

Showing results (41-50 of 109) with videos related to

Pageof 11
Sort By:
Analytical Chemistry|April 2, 2002
Improved sensitivity of a histamine sensor using an engineered methylamine dehydrogenaseLili Bao, Dapeng Sun, Hiroyasu Tachikawa, et al.
Biochemistry|November 17, 2009
Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligandsRong Fu, Fange Liu, Victor L Davidson, et al.
Archives of Biochemistry and Biophysics|November 18, 2005
The ligand geometry of copper determines the stability of amicyaninJohn K Ma, G Reid Bishop, Victor L Davidson
Biochemistry|July 3, 2007
Correlation of rhombic distortion of the type 1 copper site of M98Q amicyanin with increased electron transfer reorganization energyJohn K Ma, F Scott Mathews, Victor L Davidson
Bioorganic Chemistry|August 3, 2014
Mechanisms for control of biological electron transfer reactionsHeather R Williamson, Brian A Dow, Victor L Davidson
The Journal of Biological Chemistry|April 3, 2020
Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidaseKyle J Mamounis, Erik T Yukl, Victor L Davidson
Biochemistry|January 29, 2008
Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinoneXianghui Li, Rong Fu, Aimin Liu, et al.
Biochemistry|September 1, 2009
Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucineMoonsung Choi, Narayanasami Sukumar, Aimin Liu, et al.
Journal of Inorganic Biochemistry|June 13, 2022
Substitution of the sole tryptophan of the cupredoxin, amicyanin, with 5-hydroxytryptophan alters fluorescence properties and energy transfer to the type 1 copper siteAnthony J Pastore, Elise Ficaretta, Abhishek Chatterjee, et al.
Biochemistry|May 11, 2005
Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupledDapeng Sun, Xianghui Li, F Scott Mathews, et al.
Pageof 11

Showing results (41-50 of 109) with videos related to

Sort By:
Pageof 11
Analytical Chemistry|April 2, 2002
Improved sensitivity of a histamine sensor using an engineered methylamine dehydrogenaseLili Bao, Dapeng Sun, Hiroyasu Tachikawa, et al.
Biochemistry|November 17, 2009
Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligandsRong Fu, Fange Liu, Victor L Davidson, et al.
Archives of Biochemistry and Biophysics|November 18, 2005
The ligand geometry of copper determines the stability of amicyaninJohn K Ma, G Reid Bishop, Victor L Davidson
Biochemistry|July 3, 2007
Correlation of rhombic distortion of the type 1 copper site of M98Q amicyanin with increased electron transfer reorganization energyJohn K Ma, F Scott Mathews, Victor L Davidson
Bioorganic Chemistry|August 3, 2014
Mechanisms for control of biological electron transfer reactionsHeather R Williamson, Brian A Dow, Victor L Davidson
The Journal of Biological Chemistry|April 3, 2020
Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidaseKyle J Mamounis, Erik T Yukl, Victor L Davidson
Biochemistry|January 29, 2008
Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinoneXianghui Li, Rong Fu, Aimin Liu, et al.
Biochemistry|September 1, 2009
Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucineMoonsung Choi, Narayanasami Sukumar, Aimin Liu, et al.
Journal of Inorganic Biochemistry|June 13, 2022
Substitution of the sole tryptophan of the cupredoxin, amicyanin, with 5-hydroxytryptophan alters fluorescence properties and energy transfer to the type 1 copper siteAnthony J Pastore, Elise Ficaretta, Abhishek Chatterjee, et al.
Biochemistry|May 11, 2005
Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupledDapeng Sun, Xianghui Li, F Scott Mathews, et al.
Pageof 11