Biochemical characterization of ferredoxin-NADP(+) reductase interaction with flavodoxin in Pseudomonas putida
- Authors
- Yeom, Jinki; Park, Woojun
- Issue Date
- 31-8월-2012
- Publisher
- KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
- Keywords
- Ferredoxin-NADP(+) reductase; Flavodoxin; Isothermal titration calorimetry; Protein-protein interaction; Pseudomonas putida KT2440
- Citation
- BMB REPORTS, v.45, no.8, pp.476 - 481
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- BMB REPORTS
- Volume
- 45
- Number
- 8
- Start Page
- 476
- End Page
- 481
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/107676
- DOI
- 10.5483/BMBRep.2012.45.8.071
- ISSN
- 1976-6696
- Abstract
- Flavodoxin (Fld) has been demonstrated to bind to ferredoxin-NADP(+) reductase A (FprA) in Pseudomonas putida. Two residues (Phe(256), Lys(259)) of FprA are likely to be important for interacting with Fld based on homology modeling. Site-directed mutagenesis and pH-dependent enzyme kinetics were performed to further examine the role of these residues. The catalytic efficiencies of FprA-Ala(259) and FprA-Asp(259) proteins were two-fold lower than those of the wild-type FprA. Homology modeling also strongly suggested that these two residues are important for electron transfer. Thermodynamic properties such as entropy, enthalpy, and heat capacity changes of FprA-Ala(259) and FprA-Asp(259) were examined by isothermal titration calorimetry. We demonstrated, for the first time, that Phe(256) and LYS259 are critical residues for the interaction between FprA and Fld. Van der Waals interactions and hydrogen bonding were also more important than ionic interactions for forming the FprA-Fld complex. [BMB Reports 2012; 45(8): 476-481]
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Collections - College of Life Sciences and Biotechnology > Division of Environmental Science and Ecological Engineering > 1. Journal Articles
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