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Makale detayı · 2017 · article

Chaetomium thermophilum formate dehydrogenase has high activity in the reduction of hydrogen carbonate HCO3 to formate

YÖKSİS OpenAlex Açık erişim · bronze
Yıl2017
Atıf30OpenAlex
Yüzdelik%67,1
FWCI0,471,00 = dünya ortalaması
Scopus (SJR)Q1
WoS (JCR)Q3

Veri kaynağı ayrımı

  • YÖKSİSYÖKSİS makale kaydı
  • YÖKSİS dergi adıPROTEIN ENGINEERING DESIGN SELECTION
  • Katalog eşleşmesi (ISSN)Protein Engineering, Design and Selection
  • OpenAlexOpenAlex zenginleştirmesi (özet, atıf, konular)
  • Semantic Scholaratıf sayısı (OpenAlex ile birleştirilmez)

Özet

OpenAlex İngilizce

While formate dehydrogenases (FDHs) have been used for cofactor recycling in chemoenzymatic synthesis, the ability of FDH to reduce CO2 could also be utilized in the conversion of CO2 to useful products via formate (HCOO−). In this study, we investigated the reduction of CO2 in the form of hydrogen carbonate (HCO3−) to formate by FDHs from Candida methylica (CmFDH) and Chaetomium thermophilum (CtFDH) in a NADH-dependent reaction. The catalytic performance with HCO3− as a substrate was evaluated by measuring the kinetic rates and conducting productivity assays. CtFDH showed a higher efficiency in converting HCO3− to formate than CmFDH, whereas CmFDH was better in the oxidation of formate. The pH optimum of the reduction was at pH 7–8. However, the high concentrations of HCO3− reduced the reaction rate. CtFDH was modeled in the presence of HCO3− showing that it fits to the active site. The active site setting for hydride transfer in CO2 reduction was modeled. The hydride donated by NADH would form a favorable contact to the carbon atom of HCO3−, resulting in a surplus of electrons within the molecule. This would cause the complex formed by hydrogen carbonate and the hydride to break into formate and hydroxide ions.

Konular

Atıflar

OpenAlex cited_by_count. WoS veya Scopus atıf sayısı değildir; o kaynaklar için ayrı kolon yoktur.

30atıfOpenAlex · cited_by_count (önbellek / veritabanı)

Yerel katalogda bu makaleye atıf yapan 32 yayın (OpenAlex referans eşleşmesi; tam dünya listesi değildir).

  1. 2021 The challenges of using NAD+-dependent formate dehydrogenases for CO2 conversionAtıf 55 · OpenAlex
  2. 2021 The challenges of using NAD+-dependent formate dehydrogenases for CO2 conversionAtıf 55 · OpenAlex
  3. 2020 Engineered Formate Dehydrogenase from Chaetomium thermophilum, a Promising Enzymatic Solution for Biotechnical CO2 FixationAtıf 50 · OpenAlex
  4. 2021 Enzymes for Efficient CO2 ConversionAtıf 49 · OpenAlex
  5. 2021 Enzymes for Efficient CO2 ConversionAtıf 49 · OpenAlex
  6. 2021 Enzymes for Efficient CO2 ConversionAtıf 49 · OpenAlex
  7. 2018 Functional effects of active site mutations in NAD+-dependent formate dehydrogenases on transformation of hydrogen carbonate to formateAtıf 35 · OpenAlex
  8. 2018 Functional effects of active site mutations in NAD+-dependent formate dehydrogenases on transformation of hydrogen carbonate to formateAtıf 35 · OpenAlex
  9. 2018 Functional effects of active site mutations in NAD -dependent formate dehydrogenases on transformation of hydrogen carbonate to formateAtıf 35 · OpenAlex
  10. 2019 Tuning dimeric formate dehydrogenases reduction/oxidation activities by immobilizationAtıf 30 · OpenAlex

Yazarlar

7
  1. Aşkın Sevinç Aslan 1
  2. Jarkko Valjakka 2
  3. Jouni Ruupunen 3
  4. DENİZ YILDIRIM ÇUKUROVA ÜNİVERSİTESİ 4
  5. Nicholas J Turner 5
  6. Ossi Turunen 6
  7. BARIŞ BİNAY GEBZE TEKNİK ÜNİVERSİTESİ 7