Earticle

초록

영어

Ferredoxin-NADP+ reductase (Fpr) is known to control NADP+/NADPH pool in bacteria. Interestingly, P. putida have two Fpr (FprA, FprB) and its two cognate [2Fe-2S] Ferredoxins (FdA, FdB). Kinetic study of each Fpr was performed using a variety of assays [diaphorase, cytochromeC and ferric reductase assay]. Yeast two-hybrid was used to determine in vivo interaction between Fpr and Fd. Likewise Fpr of other bacteria, both FprA and FprB can use DPIP and ferricyanide as the terminal electron acceptor, which indicated that both Fprs have diaphorase activity. We confirmed that both Fpr products prefer NADPH to NADH at the redox complex formation. In the cytochromeC and ferric reductase assay, complex between FprB and FdA has high catalytic activity (kcat/Km) which is 5-fold higher than that of other redox couples. Similarly, In vivo interaction study using yeast two hybrid system confirms that FprB has more specific binding activity with FdA than with FdB. The data shows that specific interaction between Fpr and its cognate partner is required for efficient catalytic function. This work was supported by a NCRC grant (R15-2003-012-02002-0) and a grant (R0503443) from the BioGreen21 program

저자

• Jinki Yeom [ Division of Environmental Science and Ecological Engineering, Korea University ]
• Woojun Park [ Division of Environmental Science and Ecological Engineering, Korea University, ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576