Notable deuterium effect on the electron transfer rate of myoglobin.
The electron transfer reaction of wild-type myoglobin at an electrode was significantly facilitated in a D2O buffer as compared with that in an H2O buffer, with k(0)'(H2O)/k(0)'(D2O)= 0.13, while a minimal deuterium kinetic isotope effect on the myoglobin with modification at distal histidine (His-64) was observed.
Mie
Yasuhiro
Y
National Institute of Advanced Industrial Science and Technology, 2-17-2-1, Tsukisamu-higashi, Sapporo, 062-8517, Japan. yasuhiro.mie@aist.go.jp
Yamada
Chiho
C
Uno
Tadayuki
T
Neya
Saburo
S
Mizutani
Fumio
F
Nishiyama
Katsuhiko
K
Taniguchi
Isao
I
D000818:Animals; D002021:Buffers; D017666:Deuterium Oxide / Q000737:chemistry*; D004566:Electrodes; D004579:Electron Transport; D007700:Kinetics; D009211:Myoglobin / Q000737:chemistry*; D013552:Swine
D002021:Buffers; D009211:Myoglobin; D017666:Deuterium Oxide