Notable deuterium effect on the electron transfer rate of myoglobin
Literature Information
Yasuhiro Mie, Chiho Yamada, Tadayuki Uno, Saburo Neya, Fumio Mizutani, Katsuhiko Nishiyama, Isao Taniguchi
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 k0′H2O/k0′D2O = 0.13, while a minimal deuterium kinetic isotope effect on the myoglobin with modification at distal histidine (His-64) was observed.
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![N-[4-(Cyanoethynyl)phenyl]-16-oxo-4,7,10,13-tetraoxa-17-azahenicos-1-yn-21-amide structure N-[4-(Cyanoethynyl)phenyl]-16-oxo-4,7,10,13-tetraoxa-17-azahenicos-1-yn-21-amide structure](https://static.chemtradehub.com/structs/218/2183440-36-8-68cb.webp)

amine structure [(2-chlorophenyl)methyl](ethyl)amine structure](https://static.chemtradehub.com/structs/629/62924-61-2-0728.webp)
