کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10574335 | 976550 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Direct electrochemistry of engineered cytochrome b562 molecules with a ligand binding pocket
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی معدنی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The rapid and reversible electron transfer reaction of cytochrome b562 was observed at an In2O3 electrode. The estimated heterogeneous electron transfer rate constant (k0â²) was k0â²Â â¥Â 5.0 Ã 10â3 cm sâ1 at pH 6.5. When the methionine-7 (Met-7) residue, which coordinates to the heme iron as an axial ligand, of the wild-type cytochrome b562 was replaced by an Ala or Gly residue, a water molecule bound to the heme iron and the electron transfer rate constants decreased to 1.3 Ã 10â3 and 1.8 Ã 10â3 cm sâ1, respectively. This decrease in the electron transfer rate would be due to the larger reorganization energy for the structural change at the redox site. The midpoint potential of cytochrome b562 was shifted negatively by â¼135 mV by replacing Met-7 with Ala or Gly. Similar dissociation kinetics of cyanide for the mutated molecules as compared to native myoglobin was obtained.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Inorganic Biochemistry - Volume 99, Issue 5, May 2005, Pages 1245-1249
Journal: Journal of Inorganic Biochemistry - Volume 99, Issue 5, May 2005, Pages 1245-1249
نویسندگان
Yasuhiro Mie, Fumio Mizutani, Tadayuki Uno, Chiho Yamada, Katsuhiko Nishiyama, Isao Taniguchi,