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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 histid...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2005-01 (2), p.250-252
Main Authors: Mie, Yasuhiro, Yamada, Chiho, Uno, Tadayuki, Neya, Saburo, Mizutani, Fumio, Nishiyama, Katsuhiko, Taniguchi, Isao
Format: Article
Language:English
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Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/b413100b