Electronic Resource
Kinetics of NADP+/NADPH reduction–oxidation catalyzed by the ferredoxin-NAD(P)+ reductase from the green sulfur bacterium Chlorobaculum tepidum
العنوان: | Kinetics of NADP+/NADPH reduction–oxidation catalyzed by the ferredoxin-NAD(P)+ reductase from the green sulfur bacterium Chlorobaculum tepidum |
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المؤلفون: | Seo, Daisuke, Kitashima, Masaharu, Sakurai, Takeshi, Inoue, Kazuhito |
بيانات النشر: | Springer Science+Business Media 2017-10-03 2016-12-01 |
نوع الوثيقة: | Electronic Resource |
مستخلص: | Ferredoxin-NAD(P)+ oxidoreductase (FNR, [EC 1.18.1.2], [EC 1.18.1.3]) from the green sulfur bacterium Chlorobaculum tepidum (CtFNR) is a homodimeric flavoprotein with significant structural homology to bacterial NADPH-thioredoxin reductases. CtFNR homologs have been found in many bacteria, but only in green sulfur bacteria among photoautotrophs. In this work, we examined the reactions of CtFNR with NADP+, NADPH, and (4S-2H)-NADPD by stopped-flow spectrophotometry. Mixing CtFNRox with NADPH yielded a rapid decrease of the absorbance in flavin band I centered at 460 nm within 1 ms, and then the absorbance further decreased gradually. The magnitude of the decrease increased with increasing NADPH concentration, but even with ~50-fold molar excess NADPH, the absorbance change was only ~45 % of that expected for fully reduced protein. The absorbance in the charge transfer (CT) band centered around 600 nm increased rapidly within 1 ms, then slowly decreased to about 70 % of the maximum. When CtFNRred was mixed with excess NADP+, the absorbance in the flavin band I increased to about 70 % of that of CtFNRox with an apparent rate of ~4 s−1, whereas almost no absorption changes were observed in the CT band. Obtained data suggest that the reaction between CtFNR and NADP+/NADPH is reversible, in accordance with its physiological function. © 2016 Springer Science+Business Media Dordrecht Embargo period 12 months |
مصطلحات الفهرس: | Adrenodoxin, Charge transfer complex, Flavoenzyme, Kinetic isotope effect, Putidaredoxin, Stopped flow, Journal Article, AM |
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الاتاحة: | Open access content. Open access content |
ملاحظة: | English |
Other Numbers: | JPNII oai:irdb.nii.ac.jp:01288:0000255208 AA00362200 0166-8595 Photosynthesis Research, 130(1-3), 479-489 1389653103 |
المصدر المساهم: | NATIONAL INST OF INFO From OAIster®, provided by the OCLC Cooperative. |
رقم الانضمام: | edsoai.on1389653103 |
قاعدة البيانات: | OAIster |
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