کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10796098 | 1052692 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli](/preview/png/10796098.png)
چکیده انگلیسی
Transhydrogenase (E.C. 1.6.1.1) couples the redox reaction between NAD(H) and NADP(H) to the transport of protons across a membrane. The enzyme is composed of three components. The dI and dIII components, which house the binding site for NAD(H) and NADP(H), respectively, are peripheral to the membrane, and dII spans the membrane. We have estimated dissociation constants (Kd values) for NADPH (0.87 μM), NADP+ (16 μM), NADH (50 μM), and NAD+ (100-500 μM) for intact, detergent-dispersed transhydrogenase from Escherichia coli using micro-calorimetry. This is the first complete set of dissociation constants of the physiological nucleotides for any intact transhydrogenase. The Kd values for NAD+ and NADH are similar to those previously reported with isolated dI, but the Kd values for NADP+ and NADPH are much larger than those previously reported with isolated dIII. There is negative co-operativity between the binding sites of the intact, detergent-dispersed transhydrogenase when both nucleotides are reduced or both are oxidised.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1708, Issue 3, 15 July 2005, Pages 404-410
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1708, Issue 3, 15 July 2005, Pages 404-410
نویسندگان
Tania Bizouarn, Gijs I. van Boxel, Tina Bhakta, J. Baz Jackson,