Energetic basis on interactions between ferredoxin and ferredoxin NADP⁺ reductase at varying physiological conditions

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• 作者：Misaki Kinoshita^a ; Ju Yaen Kim^a ; Satoshi Kume^b ; Yuxi Lin^a ; K. Hun Mok^c ; Yosky Kataoka^b ; Koichiro Ishimori^d ; Natalia Markova^e ; Genji Kurisu^a ; Toshiharu Hase^a ; Young-Ho Lee^a ; ^{mr0505@protein.osaka-u.ac.jp}
• 关键词：Binding thermodynamics ; Calorimetry ; Driving force plot ; Electron transfer complex ; Ferredoxin ; Ferredoxin-NADP+ reductase
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：22 January 2017
• 年：2017
• 卷：482
• 期：4
• 页码：909-915
• 全文大小：1889 K
• 卷排序：482

文摘

Energetics of Fd:FNR binding were examined by considering physiological conditions. NaCl and pH affect energetically Fd:FNR binding with minimal effects of temperature. Enthalpy and heat capacity may modulate binding kinetics and modes for FNR activity. Entropy drives complexation by overcoming unfavorable enthalpy and tunes affinity. Driving force plot reveals condition-dependent energetic interplays for complexation.